living organisms interact to maintain and

perpetuate life animated solely by the physical

BIOCHEMISTRY LECTURE and chemical laws that govern the nonliving
universe.
TOPIC OUTLINE
HISTORY OF BIOCHEMISTRY
➢ Introduction to Biochemistry ➔ 1780s: Antoine Lavoisier proposed that the
➢ Properties of Water combustion of a candle is similar to the
➢ Chemical Reactions that occur in the respiration of animals, as both need
cell oxygen.
➢ Carbohydrates ➔ 1810s –1830s : A major substance from
➢ Reducing and Non-Reducing Sugars animals and plants was identified.
➢ Digestion of Carbohydrates ● In 1938, it was called “Protein”.
➔ 1850s –1890s: Carbohydrates, lipids, and
➢ Diseases associated with
nucleic acids were recognized.
carbohydrates
➔ 1893: Eduard Buchner demonstrated
➢ Lipids
alcoholic fermentation in cell-free yeast
➢ Lipids Digestion extracts
➢ Diseases associated with lipids ➔ 1903: The term “Biochemistry” was coined
➢ Protein Carl Neuber.
➢ Protein Digestion ➔ 1953: The Miller-Urey experiment showed
➢ Diseases associated with proteins that a variety of organic molecules,
including the amino acids could form in an
INTRODUCTION TO BIOCHEMISTRY early, reducing atmosphere.

DEFINITION
MILLER-UREY EXPERIMENT
Biochemistry is a special branch of organic
Experiments recreating the atmosphere of
chemistry that deals with matter inside the living
primitive earth have led to the spontaneous
cell.
formation of amino acids and other biological
It deals with the reactions, processes, and
molecules.
metabolism of molecules found in the body.
It shows the delicate balance of anabolism
and catabolism.
It provides fundamental understanding of
the molecular basis for the function (and
malfunction) of living things.

ORIGIN OF LIFE
● Cataclysmic eruption of hot, energy-rich
subatomic particles
● Formation of simple elements (hydrogen
and helium)
● Formation of stars
● Explosion of supernovae and release of
energy needed to fuse simpler atomic MAJOR BREAKTHROUGHS IN BIOCHEMISTRY
nuclei into more complex elements 1. The discovery of the roles of enzymes as
● Formation of life catalysts
2. The role of nucleic acids as information-carrying
The study of biochemistry shows how the molecules
collections of inanimate molecules that constitute
BUCHNER’S EXPERIMENT
Buchner showed that extracts of dead yeast cells
could convert sugar to alcohol.
JAMES SUMNER
Sumner isolated crystals from jack beans.
Continued research showed that the crystals were
composed of a pure form of urease and that
urease is a protein.
GRIFFITH’S EXPERIMENT – TRANSFORMATION PRINCIPLE
Transformation allows a bacterium to take up
genes from its surrounding environment, which
could lead to acquisition of new genetic
characteristics.
AVERY, MCCARTY AND MACLEOD
❖ Lipids and carbohydrates were removed
from a solution of heat-killed S cells
❖ Subject the solution to enzyme treatments
❖ Add a small portion of each sample to a
culture containing R cells
❖ Test for the presences of virulent S cells
HERSHEY-CHASE EXPERIMENT
Hershey-Chase experiment helped confirm that
DNA is the genetic material
PRINCIPAL AREAS OF BIOCHEMISTRY
Molecular Biology – deals with the composition,
structure and interactions of cellular molecules
that carry out the biological processes essential
for the cell's functions and maintenance.
Metabolism – the totality of chemical reactions
that occur in living matter.
Molecular Genetics – the chemistry of processes
and substances that store and transmit biological
information
Structural Chemistry – deals with the relationship
of the chemical structure and biological function.
Pharmacology – The study of drugs, their sources,
their nature, and their properties.
Immunology – deals with physiological functioning
of the immune system
MAJOR BIOMOLECULES
1. Carbohydrates
2. Lipids
3. Proteins
 PROPERTIES OF WATER A water molecule has two hydrogen atoms
Water covalently bonded to an oxygen
◎ The predominant chemical component of living ◉ Water has positive and negative ends
organisms. ◉ Water molecules are also attracted to other
◎ Odorless, colorless, and tasteless polar molecules and to ions.
￮ Hydrophilic
◎ Boiling point - 100°C (at sea level)
￮ Hydrophobic
◎ Freezing point - 0°C
◎ Water is the only substance that occurs
naturally as a solid, a liquid and a gas.
◎ Universal solvent
◎ Most of the major components of cells are
dissolved in water
◉ Proteins
◉ DNA
◉ Polysaccharides

★ 332,500,000 mi3 - Approximately 70% of

the earth is covered by water Cohesive and Adhesive
★ 97.5% is saltwater undrinkable Surface tension
★ 0.01% of freshwater - Accessible surface Capillary action
freshwater
★ 2.5% is freshwater - 77% of freshwater is Cohesion
frozen The attraction of molecules for other molecules of
the same kind
◉ Water molecules have the ability to form
hydrogen bonds with one another.
◉ Surface tension - the tendency of a liquid’s
surface to resist rupture when placed under
tension or stress

Function of Water in Body Fluid Compartments

◎ Essential constituent of all living cells
◎ Medium
◉ chemical and enzymatic action
◉ physical processes i.e. diffusion, osmosis
and filtration
◉ regulation of pH and osmotic pressure
◎ Vehicle for physiological processes
◎ Body temperature regulation
◎ Lubricant in potential spaces
◎ Refractive medium
◎ Mechanical buffer in CSF
◎ Essential for gaseous exchange in tissues and
lungs

Polar - Hydrogen bonds

Polarity of Water
 • It involves the loss of electrons

Reduction
• Occurs when a molecule gains two hydrogen
atoms and/or loses oxygen.
• It involves the gain of electrons.
● Redox reactions are common in organic
and biological chemistry, including the
combustion of organic chemicals,
respiration, and photosynthesis.
● Antioxidants are reducing agents.
● Ascorbic acid prevents damaging oxidation
of living cells.
● Tocopherol scavenges harmful by-products
Adhesion
of metabolism called free radicals.
The attraction of molecules of one kind for
molecules of a different kind
Hydrolysis
◉ Water molecules have a strong attraction to
• The reverse reaction that splits larger molecules
other molecules bearing positive or negative
to monomers.
charges.
• A water molecule is used and a covalent bond is
◉ Capillary action - Enables water to “climb”
broken
upwards through thin glass tubes
• Smaller molecules are made, or split into
monomers
Density of Water
The maximum density of water occurs at 4°C.
Condensation
◉ Between 4°C and freezing temperature, water
• A reaction that links biological molecules
becomes less dense as more of it becomes
together.
structured.
• Water molecule (H2O) is released and a new
covalent bond is formed
High specific heat - Thermal buffer
• It is also known as dehydration.
Specific heat
• A larger molecule, called polymer, is formed
The amount of energy required to change the
depending on the monomer:
temperature of a substance
• Amino acid = peptide
◉ Water can absorb a lot of heat with little change
• Nucleotide = RNA/DNA
in temperature
• Monosaccharide = polysaccharide

Neutral pH - pH = 7
Hydrogenation
pH
• Two hydrogen atoms are added across the
◎ A measure of how acidic or basic a substance
double bond of an alkene, resulting in a saturated
is.
alkane.
◎ A measure of the relative amount of free
• It is used in the food industry to make spreads
hydrogen and hydroxyl ions in the water.
and shortenings from liquid oils.
￮Water dissociates into anions (OH-) and
• Hydrogenation is also used in coal processing.
cations (H+) H3O+

Dehydrogenation
CHEMICAL REACTIONS THAT OCCUR IN THE CELL
• Dehydrogenation is the process by which
REDOX hydrogen is removed from an organic compound
Oxidation to form a new chemical.
• Occurs when a molecule loses two hydrogen
atoms and/or gains an oxygen.
• Conversion of saturated into unsaturated ●Prevention of the degradation of
compounds. skeletal muscle and other tissues
• It is used to produce aldehydes and ketones by such as the heart, liver, and
the dehydrogenation of alcohols. kidneys.
❖ Carbohydrate functions as Hormone
Tautomerism ● Many Hormones like FSH
• a phenomenon where a single chemical (Follicular Stimulating Hormone
compound tends to exist in two or more which takes part in ovulation in
interconvertible structures that are different in females) and LH (Leutinizing
terms of the relative position of one atomic Hormone) are glycoprotein and
nucleus which is generally the hydrogen. help in reproductive processes.
• It is the interconversion of aldehyde/ketone to
alcohol.

OTHER CHEMICAL REACTIONS THAT

OCCUR IN THE CELL
● Carboxylation – The addition of carboxyl group
(COOH)
● Decarboxylation – The removal of carbon
dioxide (CO2)
● Phosphorylation – The addition of a phosphate
group (PO4) MONOSACCHARIDES
● Dephosphorylation – The removal of a
phosphate group ➔ The simplest carbohydrates
➔ White, crystalline solids that contain a
single aldehyde or ketone functional
CARBOHYDRATES group.
● Carbohydrates are the most abundant ➔ The most common monosaccharides
organic molecules in nature have three to nine carbon atoms.
➔ Simple sugars
● Pure carbohydrates contain C, H, and O
➔ Cannot be further hydrolyzed
atoms ➔ Soluble in water
● “Hydrates of carbon” ➔ Sweet tasting
● Aldehyde or ketone compounds with
multiple hydroxyl groups According to Functional Group
Aldose
● Monosaccharides
Ketose
● Carbohydrates are polyhydroxy aldehydes
or ketones, or compounds that can be According to Number of Carbons
hydrolyzed to them. Triose
● Also called sugars and starches ● dihydroxyacetone, glyceraldehyde
● Animals get their carbohydrates by eating Tetrose
● erythrose, threose, erythrulose
plants, but they do not store much of what
Pentose
they consume. ● ribose, arabinose, xylose, lyxose
Hexose
Functions of Carbohydrates ● glucose, galactose, mannose, fructose
❖ Provides energy
❖ Energy storage Fischer Projection
❖ Structural
❖ Sparing Protein and Preventing Ketosis
● Regular intake of carbohydrates
will prevent protein from being used
as an energy source.
 •In plants, it is stored as starch

Fructose
•Also known as levulose
•Fruit sugar
•Sweetest monosaccharide
•It is also found in honey
•It is one of the three dietary monosaccharides,
along with glucose and galactose, that are
absorbed directly into the bloodstream during
digestion.

Haworth Projection Galactose

•One of the components of lactose, milk sugar
•It is also found in peas
•Patients with galactosemia lack an enzyme
needed to metabolize galactose.
➔ Mental retardation
➔ Failure to grow
➔ Formation of cataracts
➔ Cirrhosis
➔ Death by liver damage.
Examples of Monosaccharides
● Glucose Ribose
● Fructose •Backbone for RNA and DNA
● Galactose •D-ribose is also important in the creation of ATP
● Ribose •Obtained by the hydrolysis of RNA
● Xylose •Used to improve athletic performance and the
● Arabinose
ability to exercise by boosting muscle energy.
•Improve symptoms of chronic fatigue syndrome
(CFS), fibromyalgia, and coronary artery disease.

Xylose
• Aldopentose
• Isolated from wood.
• D-Xylose is a sugar widely used as a diabetic
sweetener in food and beverage.
• Xylose has also been used as a diagnostic agent
to observe malabsorption.
•Reduction of xylose → xylitol
Examples of Monosaccharides
Glucose
•Also known as dextrose Disaccharides
•Blood sugar
➔ Composed of two monosaccharides
•Most abundant monosaccharide
connected by a glycosidic bond
•Source of energy ➔ The glycosidic linkage joining the two
•One of the main products of photosynthesis rings can be alpha (α) or beta (β).
•Starts cellular respiration ➔ If the bond is α, the glycosidic bonds
•Excess glucose is stored as glycogen or as fat point down.
 ➢ ice crystal growth
➔ If the bond is β, the glycosidic bonds
point up. • Retention of skin moisture
➔ Hydrolysis cleaves the glycosidic bond
and forms two monosaccharides Gentiobiose
• A white crystalline solid that is soluble in water or
Sucrose hot methanol.
•Table sugar • It is composed of two glucose units
•Composed of glucose and fructose • It is one of the products that form when glucose
•Extracted from either sugar cane or beets. is caramelized by heating
•The sweetest of the disaccharides. ➢ Has a distinctive bitter note
•In recent years, sucrose has been replaced in
many commercial products by corn syrup, which is
obtained when the polysaccharides in cornstarch Polysaccharides
are broken down.
•Sucrose contains many calories.
➢ To reduce caloric intake, many artificial
sweeteners have been developed

Lactose
•Milk sugar
•Composed of glucose and galactose
•Infants have a special enzyme known as lactase
that helps digest lactose.
•As they grow older, many people lose the ability
to digest lactose and cannot tolerate milk or milk
➔ Polysaccharides contain three or more
products.
monosaccharides joined together.
•Individuals who are lactose intolerant no longer ➔ The polysaccharides serve two principal
produce lactase functions.
➢ abdominal cramps 1. To store glucose as a source of
➢ diarrhea future food energy
ex. Starch, glycogen, dextran
Maltose 2. To provide some of the
mechanical structure of cells.
•Malt sugar
ex. Cellulose,Chitin,
•Formed when starch breaks down Glycosaminoglycans,Hyaluronate
•An important component of the barley malt used , Chondroitin, Heparin
to brew beer.
Starch
•Composed of two molecules of glucose
•Stored form of energy in plants
•Types of Starch
Trehalose
1. Amylose – a linear polymer found in algae
• Non-reducing disaccharide
and other lower forms of plants.
• It is composed of two glucose units
2. Amylopectin – the dominant form of starch
• It is the main blood sugar of insects
in the higher plants. It is a branched
• It is an energy source
polymer.
• Half as sweet as table sugar
➢ sweetener
Glycogen
• Prolong food shelf life by preventing:
•Glycogen is the major form of polysaccharide
➢ drying out
storage in animals, similar in structure to
➢ going stale
amylopectin.
➢ discoloration
•It is stored mainly in the liver and in muscle cells.
•When glucose is needed for energy, glucose ➢ Heparin – stored in the mast cells of the
units are hydrolyzed from the ends of the liver, helps prevent blood clotting.
glycogen polymer.
Dextran Reducing and Non-Reducing Sugars
•Found in yeast and bacteria.
Reducing Sugars
•Bacteria growing on the surfaces of teeth
➔ These are sugars that contain free can be
produce extracellular accumulations of dextrans,
oxidized to carboxylic acids
an important component of dental plaque.
➔ Ketoses can also be reducing sugars
•Bacterial dextrans are frequently used in
because they can be isomerized to
research laboratories as the support medium for
aldoses via an enediol
column chromatography of macromolecules.
➔ Any sugar that contains a hemi-acetal
➔ All monosaccharides are reducing sugars
Cellulose
Reducing disaccharides:
•Cellulose is an unbranched polymer made up of
● Lactose, maltose, cellobiose,
repeating glucose units joined by 1,4-β-glycosidic
gentiobiose
linkages.
➔ All polysaccharides are non-reducing
•Cellulose is found in the cell walls of all plants,
sugars
where it gives support and rigidity to wood, plant
stems, and grass.
➔ A reducing sugar is a carbohydrate that is
•The most abundant structural polysaccharide
oxidized by a weak oxidizing agent (an
•Humans do not possess the enzyme to hydrolyze
oxidizing agent capable of oxidizing
cellulose (β-glycosidase) and cannot digest it.
aldehydes but not alcohols, such as the
•Cellulose makes up the insoluble fiber in our
Tollen’s reagent) in basic aqueous
diets, which is important in adding bulk to waste to
solution.
help eliminate it more easily.
➔ generate one or more compounds
containing an aldehyde group in an
Chitin
aqueous medium.
•Chitin is a polysaccharide formed from
➔ All monosaccharides are reducing sugars
N-acetyl-D-glucosamine units joined together by
➔ All polysaccharides are non-reducing
1,4-β-glycosidic linkages
sugars
•Chitin is present in the cell walls of fungi and is
the fundamental material in the exoskeletons of
Sugar Derivatives
crustaceans, insects, and spiders.
Amino Sugars
•It is the earth’s second most abundant
● Amino sugars are chemical compounds
carbohydrate polymer.
that have a sugar backbone, in which one
•Chitin-based coatings can extend the shelf life of
of the hydroxyl groups is replaced by an
fruits, and a chitin derivative that binds to iron
amine group.
atoms in meat has been found to slow the
● Amino sugars are components of structural
reactions that cause rancidity and flavor loss.
polysaccharides and of glycosphingolipids
of membranes
Glycosaminoglycans
•Glycosaminoglycans (GAGs) are a group of
Sugar Alcohols
unbranched carbohydrates derived from
● Saccharide derivatives in which a ketone
alternating amino sugar and glucuronate units.
or aldehyde group is replaced by a
➢ Hyaluronate - extracellular fluids that
hydroxyl group.
lubricate joints and in the vitreous humor of
● Also known as polyols
the eye.
● Used as sweeteners and bulking agents.
➢ Chondroitin - a component of cartilage and
➢ Have fewer calories than regular
tendons.
sugar.
 ➢ Does not cause tooth decay Digestion of Carbohydrates
➢ Bloating Major Carbohydrates in the Human Diet
➢ Diarrhea •Starch
Mannitol •Glucose
● Occurs naturally in pineapples, olives, •Sucrose
asparagus, sweet potatoes and carrots. •Lactose
● It is extracted from seaweed. •Fructose
● 50-70 % as sweet as sugar
•Cellulose
● Lingers in the intestines for a long time
➢ Bloating Digestion of Carbohydrates
➢ Diarrhea. •Digestion of carbohydrates begins at the mouth
● It is a diuretic.
➢ Mechanical digestion
● It is used to reduce pressure and swelling ➢ Chemical digestion
around the brain and in the eyes. •The teeth tears the food into smaller pieces
● Also used to prevent or treat kidney failure. •The saliva produced by the salivary gland
contains:
Sorbitol ➢ Mucin – lubrication and dispersion
● Occurs naturally in fruits and vegetables ➢ Salivary α-amylase – partial digestion of
● It is manufactured from corn syrup carbohydrates
● 50% as sweet as sugar •Monosaccharides – no hydrolysis needed prior to
● It has less of a tendency to cause diarrhea
absorption
compared to mannitol. •Disaccharides – need intestinal surface enzymes
● It is often an ingredient in sugar-free gums and for it to be broken down to monosaccharides
candies.
•Polysaccharides
➢ In the mouth, polysaccharides are
Xylitol converted to smaller polysaccharides
● Wood sugar ➢ In the small intestine, smaller
● Occurs naturally in straw, corncobs, fruit, polysaccharides are converted into
vegetables, mushrooms and some cereals. monosaccharides
● It has the same relative sweetness as sugar. •Dietary fiber – cannot be digested
● It is found in chewing gums. ➢ Increases water absorption
● It is also used in toothpastes •The action of α-amylase is inhibited by the acidic
pH of the stomach
Lactitol •Digestion continues in the small intestine with the
● About 30-40% as sweet as sugar aid of the pancreas.
● It tastes like sugar •The pancreas produces:
● It is manufactured from milk
➢ HCO3 – neutralizes the acidic chyme
● It is often found in sugar-free ice cream, ➢ Pancreatic α-amylase – aids in complete
chocolate, hard and soft candies, baked goods, carbohydrate digestion.
sugar-reduced preserves and chewing gums. •Disaccharides are further broken down by the
enzymes attached to the brush border of the small
Isomalt intestine
● Comes from beet sugar
● 45 - 65% as sweet as sugar Absorption of Sugars
● It does not lose its sweetness or break down •Mostly an active process
during the heating process.
➢ Glucose (epithelial cells) – Na+ cotransport
● Isomalt absorbs little water, so it is often used in mechanism
hard candies, toffee, cough drops and lollipops. ➢ Fructose – Na+-independent passive
transport
•Glucose transporter has low affinity for glucose
•Glucose is immediately removed by glycogen
synthesis or other mechanism
•There is a high rate of glycogen synthesis in the
brain and liver
•Insulin – secreted by the β-cell in the pancreas,
facilitate the uptake of glucose
➢ Triggers the entry of glucose to the cell
•In the brain, liver, and RBCs, glucose uptake is
not stimulated by insulin
•In muscle and adipose tissue, the rate of glucose
Without the balance between insulin and
uptake is stimulated by insulin.
glucagon, the glucose levels become
inappropriately skewed.
Diseases associated with Carbohydrates
Diabetes
A chronic disease that occurs either when the
pancreas does not produce enough insulin or
when the body cannot effectively use the insulin it
produces. Types of Diabetes Mellitus
▸ Type 1
Diabetes Mellitus ▸ Type 2
➢ Diabetes mellitus (DM) is a metabolic ▸ Gestational
disease, involving inappropriately elevated ▸ Maturity onset diabetes of the young (MODY)
blood glucose levels. ▸ Neonatal diabetes
➢ Hyperglycaemia (hyperglycemia), or raised ▸ Wolfram Syndrome
blood sugar, is a common effect of ▸ Alström Syndrome
uncontrolled diabetes ▸ Latent Autoimmune diabetes in Adults (LADA)
▸ Type 3c diabetes
▸ Steroid-induced diabetes
▸ Cystic fibrosis diabetes

Type 1 Diabetes Mellitus

▸ Previously known as insulin-dependent, juvenile
or childhood-onset
▸ It is an autoimmune disease
INsulin and Glucagon
▸ It is characterized by deficient insulin production
➢ Blood sugar is controlled by insulin and
and requires daily administration of insulin.
glucagon
▸ Neither the cause of Type 1 diabetes nor the
➢ Produced in the islets of Langerhans in the
means to prevent it are known.
pancreas
● Insulin - beta cells
Type 2 Diabetes Mellitus
● Glucagon - alpha cells.
▸ non-insulin-dependent, or adult-onset
▸ It results from the body’s ineffective use of
insulin.
▸ This type of diabetes is largely the result of
excess body weight and physical inactivity.

Gestational Diabetes Mellitus

▸ Gestational diabetes is hyperglycemia with
blood glucose values above normal but below
those diagnostic of diabetes.
▸ It occurs during pregnancy
▸ Women with gestational diabetes are at an
increased risk of complications during pregnancy
and at delivery.
Diabetes Insipidus
▸ A rare disorder that causes the body to make
too much urine.
▸ ~19 Liters of urine a day.
▸ Polyuria
▸ Polydipsia
▸ In diabetes insipidus, the blood glucose levels
are normal
Functions of Lipids
▸ Vasopressin
Galactosemia
a rare, hereditary disorder of carbohydrate
metabolism that affects the body's ability to
convert galactose (a sugar contained in milk,
including human mother's milk) to glucose.
➔ An inherited condition in which the body is
unable to properly digest galactose, a
sugar found in all foods that contain milk.
➔ Undigested sugars build up in the blood
rather than being used for energy.
Classification of Lipids
Lactose Intolerance
A common digestive problem where the body is
unable to digest lactose, a type of sugar mainly
found in milk and dairy products.
➔ Primary lactose intolerance suffered by
adults is a direct consequence of a
decrease in the production of the lactase
enzyme after infancy.
➔ This leads to the production of various
gases
➔ May be temporary or permanent
LIPIDS
❖ A family of substances that are insoluble in
water but soluble in nonpolar solvents and
solvents of low polarity, such as diethyl
ether.
❖ They are not defined by functional groups,
thus they have a variety of structures and
functions.
❖ They contain many nonpolar C—C and
C—H bonds and few polar bonds resulting
in their water insolubility.
❖ The lipids found in biological systems are
either hydrophobic (contains only nonpolar
groups) or amphipathic, which means they
possess both polar and nonpolar groups.
1. Energy source - Lipids yield 9 kcal of
energy per gram while carbohydrates and
proteins yield only 4 kcal of energy per
gram.
2. 2. Stores energy within fat cells
(adipocytes)
3. Thermal and electrical insulators
4. Protects vital organs
5. Regulate cell membrane permeability
6. Serve as chemical messengers
7. Act as enzyme cofactors and electron
carriers
8. Hydrophobic anchors for proteins
9. Precursors of other lipids
10. Transport of other lipids
11. Emulsifying agents in the g.i. tractas
chemical messengers
Hydrolyzable Lipids Non-hydrolyzable
can be converted into Lipids Cannot be
smaller molecules by cleaved into smaller
hydrolysis molecules by
hydrolysis
Simple Lipids
● Esters of fatty acids with various
alcohols.
Triglycerides – formed from glycerol and
three molecules of fatty acids.\
Waxes - esters formed from a fatty acid
and a high molecular weight \
Fatty Acid + Alcohol

Esterification of Lipids
• Esterification is a reaction between alcohols and
carboxylic acids
• Esterification is a dehydration reaction
● cis Fatty acids have two hydrogen atoms on the
same side of the double bond, which creates a
kink in the structure
● Trans Fatty acids have two hydrogen atoms on
the opposite side of the double bond, which
results in a similar structure to that of a saturated
fatty acid.

Fatty Acids
● Fatty acids are carboxylic acids with long carbon
chains.
● Naturally occurring fatty acids have an even
number of carbon atoms. Naming Fatty Acids
● Fatty acids are unbranched carboxylic acids. ● Fatty acids can be named using a shorthand
● Apart from the -COOH group, they have no nomenclature
functional groups, except that some do have ● Number of carbons
double bonds. ● Number of double bonds
● Hydrolyzable lipids are derived from fatty acids. ● Position of the double bond
Fatty acids can be classified as saturated or ● Delta – starting from the carboxylic end (COOH)
unsaturated. ● Omega – starting from the methyl end (CH3)
• Saturated fatty acids only contain single bonds
• Unsaturated fatty acids contain at least one
double bond.
• Monounsaturated fatty acids – contains one
double bond
• Polyunsaturated fatty acids – contains two or
more double bonds

*As the number of double bonds in the fatty acid

increases, the melting point decreases.

Unsaturated fatty acids can be classified as cis

fatty acids or trans fatty acid
• Cis fatty acids are generally found in nature
• Trans fatty acids are rare and manufactured fats
which are created during hydrogenation of
polyunsaturated fatty acids
Essential Fatty Acids
● Fatty acids that cannot be produced by the body
○ alpha-linolenic acid (ALA)
○ linoleic acid (LA)
● α-linolenic acid is the parent fatty acid of the
omega-3 family
○ DHA and EPA are synthesized from ALA
● Linoleic acid is the parent fatty acid of the
omega-6 family
○ Long-chain omega-6 fatty acid and
arachidonic acid are synthesized from LA
Docosahexaenoic acid (DHA)
• DHA is a structural fat, making up approximately
30% of the structural fats in the gray matter of the
brain and 97% of the total omega-3s in the brain.
• Naturally found throughout the body and is most
abundant in the brain, eyes and heart.
• Necessary for growth and development of infants
• DHA is found in breast milk.
Eicosapentaenoic acid (EPA)
• EPA helps with childhood behavior and
academic performance.
• Precursor for the prostaglandin-3 and
thromboxane-3 families.
• Lowers serum lipid concentration
• Reduces incidence of cardiovascular disorders
• Lowers the risk of developing and worsening
cognitive decline and dementia
Essential Fatty Acids Ratio
Triglycerides
● Also known as triacylglycerols
● Includes fats and oils
● Humans store energy as triglycerides in adipose
cells below the surface of the skin, in the breast
area, and surrounding internal organs.
● Hydrolyzed by enzymes called lipases to
produce energy.
● Complete metabolism of a triacylglycerol yields:
CO2, H2O, and energy.
Fats
● A mixture of triglycerides containing a high
proportion of long-chain, saturated fatty acids
● Mostly obtained from animals
● Fats have higher melting points
● Solids at room temperature.
● Pure fat is colorless and has extremely bland
taste.
● Hydrolysis of fats by alkali is called
saponification.
Oils
● A mixture of triglycerides containing a high
proportion of long-chain, unsaturated fatty acids
○ Or short-chain, saturated fatty acids
● Oils are fats in liquid state
● Oils have lower melting points
● Liquids at room temperature.
● Mostly obtained from plants and fish
Rancidity
● Oxidative rancidity is a condition caused by fat
oxidation
○The polyunsaturated fatty acid portions
react with oxygen to form peroxides.
● Hydrolytic rancidity is a condition caused by fat
hydrolysis
○ Develops when triglycerides are
hydrolyzed and free fatty acids are released.
Waxes
● They are esters of fatty acids with high
molecular weight alcohols.
● Because of their long nonpolar C chains, waxes
are very hydrophobic.
● Form protective coating on plants and fruits, and
in animal
 Lipoproteins
● Lipoproteins are the primary means of transport
of cholesterol among tissues
● Secreted by the small intestine and liver into the
circulating blood
Complex Lipids ● Composed of lipids and special proteins
Lipids contain parts other than fatty acids and (apolipoproteins)
alcohol.
● Phospholipids
Major Groups of Lipoprotein
● Sphingolipids
● Lipoproteins 1. Chylomicron - formed in the mucosal cell of the
● Glycolipids intestine
Found in cell membranes, brain, nervous - Delivers triglycerides to the adipose
tissues, myelin sheaths of nerves, and blood tissue and muscle
platelets - Delivers dietary cholesterol to the liver
= Fatty acid + Alcohol + X 2. VLDL – formed in the liver for the export of
Phospholipids triglycerides
● Also called phosphoglycerides or - transports triglycerides from the liver to
glycerophospholipids the muscle and adipose tissue for storage
● Long chained fatty acids on a glycerol backbone or energy
attached to a phosphoric acid molecule containing 3. LDL - primary carriers of cholesterol in the
an alcohol substituent. (usually an amino alcohol) blood for delivery to the tissues
● Essential components of cell membranes and 4. HDL - scavenger for cholesterol from peripheral
are found in small concentrations in other parts of tissues
the cell. - Cholesterol is returned to the liver for
● Lecithins - Important cell membrane component. metabolism
- Easily form micelles.
● Cephalins - Found in most cell membranes
Derived Lipids
- Aid in blood clotting. ● Products of the hydrolysis of simple and
complex lipids
Sphingolipids ● These include:
● A class of lipids built from long chained fatty ▪ Fatty acids
acids attached to a sphingosine backbone rather ▪ Alcohol
than glycerol. ▪ Steroids
▪ Steroid hormones
▪ Ketone bodies,
▪ Eicosanoids
▪ Prostaglandins
▪ Fat-soluble vitamins
Steroids
● Steroids are a group of lipids whose carbon
ABO Blood Type skeletons contain several fused rings:
1. Type A - contains Antigen A (on rbc) anti-B
antibody (in plasma)
2. Type B - contains Antigen B (on rbc) anti-A
antibody (in plasma)
3. Type AB - contains Antigen AB (on rbc) no
antibody (in plasma)
4. Type O - contains no antigen (on rbc) anti-A
and anti-B antibodies (in plasma) Sterol
● Also known as steroid alcohol
● Occur naturally in plants, animals and fungi
● Plant sterols have cholesterol lowering
properties
●Plant sterols are found in grains, vegetables,
fruits, legumes, nuts, and seeds
●Plant sterols are also called phytosterols .
Cholesterol
● Elevated levels of cholesterol in the bloodstream
lead to coronary artery disease, heart attack, etc.
● Transported through the bloodstream by
lipoproteins.
● LDLs deposit cholesterol on the walls of arteries
when they carry more than is needed to form cell
membranes.
○ This forms plaque, which restricts blood flow
● HDLs reduce the level of cholesterol in the
bloodstream by bringing excess back to the liver
Atherosclerosis
● A disease caused by plaque build up in the
arteries
● Plaque or atheroma is composed of fat,
cholesterol, calcium and other substances found
in the blood.
● The plaque hardens and narrows the arteries
● Limited flow of oxygen-rich blood and increased
risk of blood clots
● It is triggered by subtle physical or chemical
insults to the endothelial layer of the arteries.
● It is the leading cause of heart attack, strokes,
and peripheral vascular disease
Bile Salts
● Bile salts are oxidation products of cholesterol.
● Bile salts are powerful detergents.
● Bile salts are found in bile
● Bile is produced in the liver and is stored in the
gallbladder
● Responsible for fat emulsification
● Secretion of bile salts and cholesterol into the
bile by liver is the onlymechanism by which
cholesterol is excreted.
Fat-Soluble Vitamins
● Vitamins are organic compounds and vital
nutrients that an organism requires in limited
amounts.
● They cannot be produced by the body.
● Fat-soluble vitamins are stored in the body for
long periods of time.
● They pose a greater risk for toxicity than
water-soluble vitamins.
● Vitamins A, D, E, K
Vitamin A
● Vitamin A is the name of a group of fat-soluble
retinoids, including retinol, retinal, and retinyl
esters.
● Two forms of vitamin A are available in the
human diet:
○ Preformed vitamin A
○ Provitamin A carotenoids.
● Preformed vitamin A is found in foods from
animal sources, including dairy products, fish, and
meat (especially liver).
● The most important provitamin A carotenoid is
beta-carotene.
● Both provitamin A and preformed vitamin A
must be metabolized intracellularly to retinal and
retinoic acid.
Functions of Vitamin A
1. Vitamin A is involved in immune function,
vision, reproduction, and cellular communication.
2. Vitamin A is an essential component of
rhodopsin. It supports the normal differentiation
and functioning of the conjunctival membranes
and cornea.
3. Vitamin A also supports cell growth and
differentiation, playing a critical role in the normal
formation and maintenance of the heart, lungs, 2. Prevents platelet aggregation.
kidneys, and other organs. 3. Balances cholesterol
4. Maintenance of normal skin and mucus 4. Repairs damaged skin.
membrane 5. Balances hormones.
5. Normal iron metabolism
Vitamin K
Vitamin D ● Naturally present in some foods and is available
● Naturally present in very few foods, added to as a dietary supplement.
others, and available as a dietary supplement. ● Three different forms: vitamin K1
● It is also produced endogenously when UV rays (phylloquinone), vitamin K2 (menaquinone) and
from sunlight strike the skin. vitamin K3 (menadione)
● It is a hormone ● Phylloquinone is present primarily in green leafy
● Vitamin D obtained from sun exposure, food, vegetables and is the main dietary form of vitamin
and supplements is biologically inert and must K.
undergo two hydroxylations in the body for ● Menaquinones, which are made by the bacteria
activation. that line the gastrointestinal tract and also found in
● The first occurs in the liver and converts vitamin fermented foods.
D to calcidiol. ● Menadione is the synthetic form of vitamin K
● The second occurs primarily in the kidney and Functions:
forms calcitriol. ● Promotes blood clotting:
Functions: ● Prevents bone breakdown by blocking
1. Promotes calcium absorption in the gut and osteoclasts
maintains adequate serum calcium and phosphate ● Strengthens bones by activating osteocalcin
concentrations which acts like a glue to help hold calcium into
2. Bone growth and bone remodeling by bones.
osteoblasts and osteoclasts. ● Prevents arteriosclerosis (or hardening of the
3. Prevents rickets in children and osteomalacia in arteries) by keeping calcium out of the arterial
adults. linings.
4. Vitamin D and calcium helps protect older ● Protects cells from oxidative stress.
adults from osteoporosis. ● Essential for the synthesis of sphingolipids
5. Modulation of cell growth, neuromuscular and
immune function, and reduction of inflammation.
6. Modulation of cell proliferation regulation,
differentiation, and apoptosis. Steroid Hormones
● Cholesterol is the starting material for the
Vitamin E synthesis of steroid hormones.
● Naturally present in some foods and is available ● Progesterone serves as the starting compound
as a dietary supplement. for both the sex hormones
● The collective name for a group of fat-soluble and the adrenocorticoid hormones
compounds with distinctive antioxidant activities ● Adrenocorticoid hormones are products of the
● Naturally occurring vitamin E exists in eight adrenal glands.
chemical forms (alpha-, beta-, gamma-, and ● Sex hormones:
delta-tocopherol and alpha-, beta-, gamma-, and o The most important male sex hormone is
delta-tocotrienol) that have varying levels of testosterone
biological activity. o The most important female sex hormone is
● α-tocopherol is the only form recognized to meet estradiol
human requirements o Estradiol and progesterone regulates the
Functions: menstrual cycle.
1. Antioxidant
Ketone Bodies
● Produced by the liver from the breakdown of
fatty acids during periods of low food intake,
carbohydrate restrictive diets, starvation,
prolonged intense exercise, or in untreated type 1
diabetes mellitus.
● Acetoacetate, beta-hydroxybutyrate, and
acetone
● Ketone bodies serve as energy source for heart,
kidney, and skeletal muscles, thereby preserving
the limited glucose for use by the brain.
● An increase in ketone bodies lowers the pH of
the blood
● Acidification of the blood impairs the ability of
hemoglobin to bind to oxygen
Eicosanoids
● Eicosanoids are metabolites of arachidonic acid
● The eicosanoids consist of the prostaglandins
(PGs), thromboxanes (TXs) leukotrienes (LTs) and
Lipoxins (LXs).
● All mammalian cells except erythrocytes
synthesize eicosanoids.
● Responsible for inflammatory responses, on the
intensity and duration of pain and fever, and on
reproductive function.
● Inhibits gastric acid secretion
● Regulates blood pressure through vasodilation
or constriction
● Inhibits or activates platelet aggregation and
thrombosis.
Prostaglandins
● Thought to be synthesized in the prostate
glands
● Plays a key role in the body’s inflammatory
response
● Triggers pain, fever and inflammation when
there is a
damaged or infected tissue
● Responsible for :
○ Constriction and dilation of blood vessels
○ Opening and closing airways
○ Contracting and relaxing smooth muscles
○ Uterine contractions
Leukotrienes
● Originated from leukocytes
● Leukotrienes are activated in response to
asthmatic and allergic reactions
● Leukotrienes are also involved in atopic
dermatitis, rheumatoid arthritis, chronic obstructive
pulmonary disease, and interstitial lung diseases.
● Cysteinyl leukotrienes – contracts smooth
muscles of the airways and stimulate mucus
secretions during allergic reactions
● Leukotriene B4 – activates the production of
inflammatory cells and cytokine
Thromboxanes
● Thromboxanes are secreted from thrombocytes
● Potent vasoconstrictors
● Stimulates platelet aggregation
● They act in the formation of blood clots and
reduce blood flow to the site of the clot.
● Thromboxane A2 – produced by activated
platelets during hemostasis
● Thromboxane B2 – inactive; precursor of TXA2
Lipoxins
● Lipoxins are endogenous anti-inflammatory,
pro-resolving molecules that play a vital role in
reducing excessive tissue injury and chronic
inflammation.
● Lipoxins regulate components of both the innate
and adaptive immune systems including
neutrophils, macrophages, T-, and B-cells.
LIPIDS DIGESTIONS
Dietary Lipids
» Triglycerides constitute ~90% of daily lipid
intake.
» The rest is made up of:
– Phospholipids,
– Cholesterol
– Cholesteryl esters
– Free fatty acids
» Fat is energy rich and provides 9 kcal/g
★ Normally essentially all (98%) of the fat
consumed is absorbed, and most is
transported to adipose for storage.
Organs involved in Lipid Digestion
Anatomical Locations Involved in Lipid Digestion»
Mouth
⋄ Mechanical digestion
⋄ Lingual lipase
» Stomach » Anchors lipase to the micelle
⋄ Mechanical digestion » Improves activity of pancreatic lipase
⋄ Gastric lipase 3. Phospholipase A2
» Small Intestine » Secreted by the pancreas into the
⋄ Cholecystokinin intestine
⋄ Pancreatic lipase » Hydrolyzes phospholipids with an
⋄ Cholesterol esterase unsaturated fatty acid on C2
⋄ Phospholipase 4. Cholesterol esterase
⋄ Milk lipase* » Hydrolyzes fatty acids from cholesterol
esters
Lipid Digestion
Minor digestion of triglycerides in the mouth and Absorption of Lipids
stomach » Most fat absorption takes place in the
» Hydrolysis of triglycerides to free fatty acids and duodenum or jejunum
diglycerides»The churning action of the stomach » Micelles carry monoglycerides and free fatty
produces small fat droplets acids to the brush border where they diffuse into
» Lingual and gastric lipases hydrolyze medium enterocytes
chain triglycerides (TAGs) » Bile salts are absorbed in the ileum
⋄ Lingual lipase is more active in infants (enterohepatic circulation)
⋄ Gastric lipase begins the actual lipid » Short and medium chain fatty acids are oxidized
digestion in the liver and used for triglyceride formation.
⋄~10-30% of TAGs are hydrolyzed » Long chain fatty acids form chylomicrons
in the stomach » Cholesterol is incorporated into micelles
Major digestion of all lipids in the small intestine » Triglycerides and cholesterol are transported by
» Major digestion of all lipids occur in the lumen of lipoproteins
the small intestine
» The presence of chyme in the small intestine
stimulates cholecystokinin to release bile from DISEASES ASSOCIATED WITH LIPIDS
gallbladder.
Obesity - abnormal or excessive fat accumulation
» Further hydrolysis of other dietary fats involves
that presents a risk to health.
pancreatic enzymes
● Adiposity
⋄ Pancreatic lipase hydrolyzes fat at 3 and
● Caused by the increase in the size and the
1 positions of the triglyceride while in the micelles.
amount of fat cells in the body.
● It can cause: metabolic syndrome, high blood
What is Bile?
pressure, atherosclerosis, heart disease, diabetes,
» It is an alkaline solution responsible for fat
high blood cholesterol, cancers and sleep
emulsification.
disorders.
» It is produced in the liver and stored in the
• Lifestyle change
gallbladder
○ Heart-healthy eating
» It is composed of:
○ Increased physical activity
⋄ Bile acids/salts Lecithin
• FDA-approved
⋄ Cholesterol Bilirubin
weight-loss medicines
• Surgery
Other Enzymes Involved in Lipid Digestion
1. Milk lipase
Hypertension - a condition in which the blood
» Small intestine
vessels have persistently raised pressure.
» Converts medium chain triglycerides into
● High blood pressure
free fatty acids and glycerol
2. Pancreatic colipase
● Blood pressure is created by the force of blood
pushing against the walls of blood vessels
(arteries) as it is pumped by the heart.
● The higher the pressure, the harder the heart
has to pump.
● < 120/80 mmHg
• Hypertension can increase the risk of heart,
brain, kidney and other diseases.
• It is a major cause of premature death
worldwide, with upwards of 1 in 4 men and 1 in 5
women – over a billion people – having the
condition.
Atherosclerosis - occurs when plaque builds up
inside arteries
● Thickening or hardening of the arteries.
● It is caused by a buildup of plaque in the inner
lining of an artery.
● Plaque is made up of deposits of fatty
substances, cholesterol, cellular waste products,
calcium, and fibrin.
• Atherosclerosis is a slow, progressive disease
• Risk factors include:
○ High cholesterol/ triglyceride levels
○ High blood pressure
○ Smoking
○ Type 1 diabetes
○ Obesity
○ Physical inactivity
○ High saturated fat die
Eye Diseases
Arcus senilis
● Annular lipid infiltration of corneal periphery.
● A gray or white arc visible above and below the
outer part of the cornea — the clear, domelike
covering over the front of the eye.
○ The arc may become a complete ring
around the iris.
● It's caused by fat (lipid) deposits
deep in the edge of the cornea.
• It is common in older adults.
○ High cholesterol
• It doesn't affect vision, nor does it require
treatment.
• It occurs in younger people who have severe
cases of high cholesterol and familial
hyperlipidemia.
○ ↑ risk of heart disease
Lipid keratopathy
● Fatty degeneration of the cornea is
characterized by whitish or yellowish deposits.
● The fat deposits mostly consist of cholesterol
and fatty acids
1. Primary form
○ usually occurs bilaterally
○ Familial HDL Deficiency
○ Lecithin Cholesterol
Acyltransferase deficiency
2. Secondary form
○ Most common form
○ Presence of corneal blood
vessels from trauma, interstitial
keratitis or herpes zoster keratitis
Blepharitis
● An inflammation of the eyelids in which they
become red, irritated and itchy with dandruff-like
scales that form on the eyelashes.
● It is a common eye disorder caused by either
bacteria or a skin condition, such as dandruff of
the scalp or rosacea.
Anterior Blepharitis
1. Bacterial (usually staphylococcal) ○ direct
infection
○ reaction to staphylococcal exotoxin
○ allergic response to staphylococcal
antigen
2. Seborrhoeic
○ Disorder of the ciliary sebaceous
glands of Zeis ■ Abnormal excessive
neutral lipids are split by Corynebacterium
acne into irritating free fatty acids
Xanthelasma
● These are creamy-yellow plaque-like lesions
which frequently involve the skin of upper and
lower lids near the inner canthus.
● It represents lipid deposits in histiocytes in the
dermis of the lid.
● It can be raised or flat
• It can be a sign of heart disease.
• Xanthelasma is also more common in women
and those of Asian or Mediterranean descent.
• Who are at risk?
○ Smokers
○ Overweight
○ High blood cholesterol
○ High blood pressure or diabetes
 PROTEINS
› A group of complex organic macromolecules that
contain carbon, hydrogen, oxygen, nitrogen, and
usually sulfur
› Linear polymers of amino acids connected by
peptide bonds
› Diverse abundant class of biomolecules
› The most important of all biological compounds
› Derived from the Greek word proteios, which
means first of importance
› Constitutes about 50% of the dry weight of cells
› Unlike lipids and carbohydrates, proteins are not
stored, so they must be consumed daily.
› Current recommended daily intake for adults is
0.8 grams of protein per kg of body weight
› Dietary protein usually comes from eating meat
and dairy products.
What makes up proteins?
Amino Acids
Most amino acids are chiral molecules
› Chiral carbon centers are carbon atoms that are
attached to four different substituents
Most common amino acids are α-amino acids
All amino acids in the body are L-isomers › L
amino acids have the amino group on the left.
Exemptions
Glycine - It is the simplest amino acid - It is the
only achiral amino acid
Proline - It is an imino acid. - It is a secondary
amine
Amino acids are amphiprotic compounds
› They have an acidic and basic component
› Aqueous solutions of amino acids can act as
buffers
Amino acids are zwitterions
› Zwitterions have a positive and a negative end
› Zwitterions are neutral
Zwitterion can only exist at a specific pH
› Isoelectric point is a pH at which amino acids
have equal positive and negative charges
› Peptides and proteins are formed when amino
acids are joined together by amide bonds. The
amide bond is called a peptide bond.
› A dipeptide has two amino acids joined together
by one peptide bond.
› Polypeptides have many amino acids, while
proteins have more than 40 amino acids
 › There are 10 essential amino acids
Examples of amino acids Phenylalanine* Methionine**
Valine Histidine***
Threonine Arginine****
Tryptophan Leucine
Isoleucine Lysine

Formation of Peptides
Peptide bonds are formed by a condensation
reaction
› Water is removed
› If the amino acid is in zwitterion form:
1. Remove oxygen from the first amino acid.
2. Remove two hydrogens from the second amin
acid.
3. Connect the two amino acids
If the amino acid is uncharged:
1. Remove oxygen and a hydrogen from the first
amino acid.
2. Remove hydrogen from the second amino acid.
3. Connect the two amino acids
Classification of Amino Acids
1. Non-polar
- Leucine, Isoleucine, Proline, Alanine, Valine,
Methionine, Phenylalanine, Tryptophan
2. Polar uncharged (neutral)
- Glycine, Serine, Asparagine, Glutamine,
Tyrosine, Threonine, Cysteine
3. Polar acidic
- Aspartic acid, Glutamic acid
4. Polar basic
- Histidine, Lysine, Arginine
Essential amino acids
› Essential amino acids are amino acids that
cannot be produced by the body
Phenylalanine
›Production of tyrosine
›It is required if one’s diet does not contain
enough tyrosine
› Formation of neurotransmitters and hormones
• Norepinephrine
• Epinephrine
• Dopamine
• Thyroid hormones
›Helps with depression
Valine
›Promotes the repair of tissues.
›Helps with energy prevision
›Regulates blood sugar levels
›Assists with normal growth and development.
›Stimulates the central nervous system.
›Builds muscle mass
›Helps with stress management
›Regulates the immune system
Tryptophan
›Required to produce serotonin and melatonin.
›Improves sleep quality
›Supports the immune system, metabolism,
circulation, CNS, and enzyme production
›Needed for the manufacture of vitamin B3
(niacin).
›Assists with the regulation of blood sugar
›Stops free radical damage
›Prevents cholesterol buildup.
Threonine
›Helps maintain the balance of protein in the body
›Supports normal growth and development.
›Supports the central nervous system,
cardiovascular system, immune function, and liver
function.
›Produces the amino acids serine and glycine
›Helps to process fatty acids and prevent liver
failure when combined with methionine and
aspartic acid

Isoleucine
›Involved in muscle development and repair.
›Insufficient levels of this amino acid within the
body can produce symptoms that are similar to
those experienced by people suffering from
hypoglycemia.
Methionine
›Sulphur-containing essential amino acid.
›Helps in effectively processing and removing fat.
›Prevents liver damage in acetaminophen
poisoning
›Improves wound healing.
›Produces the amino acids:
•Taurine
•Cysteine
•Glutathione
Histidine
›Essential for infants to ensure the regulation of
growth and natural development and repair
mechanisms.
›Production of histamine, glutamate, ferritin and
hemoglobin.
›Essential for maintaining energy and blood
supply as well as detoxification of heavy metals.
›Regulation of the blood pH and wound healing.
Arginine
›A semi-essential amino acid.
› The rate of synthesis is too slow
›Stimulates the release of growth hormone and
insulin.
›Improves the circulation
›Strengthens the immune system
›Enhances male libido
›Accelerates the rate of wound healing
›Improves the burning of excess fat.
›Decreases cholesterol levels
›It is converted in the body into nitric oxide.
›Preterm infants are unable to synthesize arginine
Lysine
›Helps to build a healthy immune system.
›Involved in the development of antibodies and
has important antiviral properties.
›Assists with the formation of collagen and muscle
tissue.
›Aids in growth and maintenance of bones
› Lowers cholesterol
Leucine
› The 4th most concentrated amino acid found
within muscle.
›Helps to maintain nitrogen balance and energy
supply.
›Support muscle building.
›Decreases muscle wasting
› Lowers cholesterol and LDL levels
›Reduces the risk of atherosclerosis
Limiting Amino acids
› The amino acid that is in shortest supply in
relation to need.
› Limiting amino acids are found in the shortest
supply from incomplete proteins.
› Incomplete proteins are those found in plant food
sources and gelatin.
Functions of Proteins
1. Structure
› Proteins provide strength to cells and tissue
› chief constituents of skin, bones, hair, and nails.
Examples:
● Collagen
› Most abundant protein in the body.
› Its is used to make connective tissue.
› It is a major component of bone, skin,
muscles, tendons, and cartilage.
› It is composed of three chains, wound
together in a tight triple helix.
› It helps to make tissues strong and
resilient
● Keratin
› Keratins comprise the type I and type II
intermediate filament-forming proteins and
occur primarily in epithelial cells.
› Found on epithelial cells, which line the
inside and outside surfaces of the body.
 › Keratins help form the tissues of the hair, 4. Transport
nails, and the outer layer of the skin. › Proteins transport other substances
● Elastin Examples:
› Elastin is a key extracellular matrix ● hemoglobin
protein that is critical to the elasticity and › Carries oxygen from the lungs to the
resilience of many vertebrate tissues body's tissues and returns carbon dioxide
including large arteries, lung, ligament, from the tissues back to the lungs.
tendon, skin, and elastic cartilage. › Made up of four globulin chains.
● Fibroin - proteins that constitute silk fibers › Each globulin chain contains heme.
. › Responsible for the color of blood.
› Maintains the shape of the red blood
cells.
2. Catalysis ● serum albumin
› Reactions in the body are catalyzed by enzymes › Serum albumin is the largest protein
› Enzymes speed up reactions by lowering the component of human blood (50–60%)
activation energy › It is an important factor in the regulation
Examples: of plasma volume and tissue fluid balance.
Amylase ● Lipoproteins
Lipase
Protease Carbon monoxide poisoning
›Carbon monoxide (CO) is poisonous because it
3. Movement has a stronger affinity to Fe2+ than oxygen
› Muscles are made up of protein molecules ›Hemoglobin complexed with CO cannot carry
Example: oxygen, and cells will die from lack of oxygen.
● Myosin Common Sources:
› Thick filament ›House fire
› Head and tail ›Car exhaust
› Motor protein ›Boilers/furnaces
› Generates the force in a muscle ›Cigarette smoke
contraction.
● Actin 5. Hormones
› Spherical protein › Do not perform any obvious chemical
› Thin filament transformation but they regulate the ability of other
› 2 long chains proteins to carry out their physiological functions.
› Each actin has a myosin-binding site Examples:
● Tropomyosin - regulate the interaction of ● Insulin
actin and myosin ● Vasopressin
› Blocks myosin binding sites on actin › Antidiuretic hormone
molecules, preventing cross-bridge › Produced in the hypothalamus.
formation › Helps control blood pressure by acting on
› Prevents contraction in a muscle without the kidneys and the blood vessels.
nervous input › Conserves body water by reducing the
● Troponin - loss of water in urine.
› Globular protein ● Erythropoietin
› Protein complex that binds to › Glycoprotein hormone
tropomyosin › It is naturally produced by the peritubular
› Helps position tropomyosin on the actin cells of the kidney
molecule. › It acts on red blood cells to protect them
against destruction.
 › It stimulates stem cells of the bone
marrow to increase RBC production.
› EPO doping increases an athlete’s
performance ability and endurance.
● Oxytocin
› It is a neurotransmitter
› Produced in the hypothalamus
› It is released in response to activation of
sensory nerves during labor,breastfeeding,
sexual activity, positive interaction between
adults or between humans and animals.
› well-being and anti-stress effects
● Somatotropin
› Growth hormone
› Secreted by the anterior lobe of the
pituitary gland.
› It stimulates the growth of essentially all
tissues of the body.
› Keeps blood glucose levels within set
levels.
› Decreases the rate of glucose uptake
and metabolism
Melatonin
› Sleep hormone
› Initiates and maintains sleep
› Produced in response to darkness.
› Pineal gland
› Being exposed to light at night can block
melatonin production.
› It helps with sleep-wake cycle
› Circadian rhythm
› Immune system health
› Antioxidant
Dopamine
› It is a neurohormone
› Produced in the hypothalamus
› Provides an intense feeling of reward.
› Pleasure
› Addiction
› Low dopamine levels are associated with
diseases including Parkinson’s disease, restless
legs syndrome and attention deficit hyperactivity
disorder (ADHD).
› It influences learning, memory, happiness as well
as regulating body temperature, sleep, sexual
behavior and hunger.
› Lack of enough serotonin is thought to play a
role in depression, anxiety, mania and other health
conditions.
6. Protection
› When a protein from an outside source or some
other foreign substance (antigen) enters the body,
the body makes its own proteins (antibodies) to
counteract the foreign protein.
Example:
● Immunoglobulin
● Fibrinogen
● Thrombin
7. Storage
› Proteins provide a reservoir of an essential
nutrient
› They also provide sufficient nitrogen in times of
need
Example:
● Ovalbumin
› The major egg white protein synthesized
in the hen's oviduct
› It is responsible for egg white formation.
› It accounts for about 54% of the total
proteins of egg albumen.
● Casein
● Ferritin
› Ferritin is a protein complex that stores
iron in a soluble, non-toxic form.
› Low levels of ferritin lead to
iron-deficiency anemia.
› High levels of ferritin can damage your
joints, heart, liver, and pancreas.
Myoglobin
› Monomeric protein found mainly in muscle tissue
› It serves as an intracellular storage site for
oxygen.
› The primary function of myoglobin is to supply
oxygen to the muscle.

Serotonin Levels of Protein Structure

› It is a neurohormone 1. Primary Structure
› Mostly found in the gut – Linear sequence of amino acids
– a small protein has at least 60 amino acids › More sensitive to changes in pH and
residues temperature
– Connected by peptide bonds › More or less soluble to water

2. Secondary Structure According to Composition

– A repetitive conformation of the protein 1. Simple Proteins
backbone – composed of amino acids
– Connected by peptide bond and hydrogen – also called homoproteins
bonds Examples: albumins, globulins, glutelins,
– alpha-helix; beta pleated; random coil albuminoids, histones, protamines, collagen, and
keratin
3. Tertiary structure
– The complete 3D arrangement of 2. Conjugated Proteins
the atoms in a protein – contains a prosthetic group or a non-protein part
– Held together by: in addition to protein.
peptide bonds Examples: Glycoprotein, Phosphoprotein,
hydrogen bonds Lipoprotein, Chromoprotein
disulfide bonds
salt bridges 3. Derived Proteins
- Proteins derived from simple or conjugated
4. Quaternary structure proteins by physical or chemical means.
– The spatial relationship and interactions Examples: denatured proteins and peptides
between subunits in a protein that has more than
one polypeptide chain According to Nutritional Basis
– Held together by peptide bonds, hydrogen 1. Complete Proteins
bonds, disulfide bonds, salt bridges – Contains an adequate amount of all the
essential amino acids that should be incorporated
in the diet
– Even if the protein contains all the essential
amino acids, they must be in equal proportion in
order to be considered complete
– Generally comes from animal and fish products
Source: meat, fish, dairy, egg

2. Incomplete Proteins
– Any protein that lack one or more essential
Classification of Proteins amino acids in correct proportion
According to Shape – Also called partial proteins
Fibrous Source: grains, nuts, beans, seeds, peas, corn
› Long and narrow – Combining two or more incomplete proteins to
› Used mainly for structural purposes create a complete protein
› Repetitive amino acid sequences ★ Complementary proteins compensate for
› Less sensitive to changes in pH and temperature each other’s lack of amino acids
› Insoluble to water
Properties of protein
Globular Protein Denaturation
› Round / spherical – the loss of the secondary, tertiary and
› Used for non-structural purposes quaternary structures of a protein by a chemical or
› Irregular amino acid sequence a physical agent
– the primary structure remains intact ○ Acinar cells - Proelastase
○ Trypsin
● Carboxypeptidase
○ Pancreas - Procarboxypeptidase
○ Aromatic amino acids
○ Branched amino acids
● Aminopeptidase
○ Small intestine - Proaminopeptidase

\
Factors that Cause Protein Denaturation
1. Heat – cleaves hydrogen bonds
2. Detergents – opens up hydrophobic regions
3. Acids and bases – affects salt bridges and
H-bonds
4. Salts – affects salt bridges and H-bonds
5. Reducing agents – breaks disulfide bonds
6. Heavy metal ions – attacks SH group
7. Alcohol – Hydrogen bonds
8. Mechanical Stress
Digestion of Proteins
Protein Hydrolysis ● Digestion of proteins begins in the stomach
›Protein hydrolysis involves breaking the peptide ○ HCl denatures proteins
bonds by treatment with aqueous acid, base, or ○ Pepsin cuts proteins into smaller
certain enzymes. polypeptides
›The primary structure of protein is cleaved by the ● The small intestine releases hormones to
addition of water stimulate the digestive process
○ Secretin - Sodium bicarbonate
PROTEIN DIGESTION ○ Cholecystokinin - pancreatic enzymes
Organs involved in Protein Digestion ● Majority of protein digestion occurs in the small
● Stomach intestine
○ Start of protein digestion
● Pancreas Absorption of Proteins
● Small Intestine ● In adults, essentially all protein is absorbed as
○ Major digestion of protein tripeptides, dipeptides or amino acids
○ Duodenum
Enzymes involved in Protein Digestion ○ Facilitated diffusion or active process
● Pepsin ● Amino acids are transported to the liver via the
○ Gastric chief cells - pepsinogen hepatic portal vein
■ Acetylcholine ○ Enterohepatic circulation
■ Gastrin
■ pH 1.5 - 2.0 DISEASES ASSOCIATED WITH PROTEINS
● Trypsin Protein Deficiency - state of relative or absolute
○ Pancreas - Trypsinogen deficiency of body 1 proteins or one or more of the
○ Enterokinase (Positive feedback) essential amino acids.
● Chymotrypsin ▫ Hypoproteinemia
○ Pancreas - Chymotrypsinogen ▫ A state of relative or absolute deficiency
○ Trypsin of body proteins or one or more of the
● Elastase essential amino acids.
 ▫ Rare in developed countries ▫ Previously believed to be due to protein
deficiency and low levels of antioxidants and
Signs of protein deficiency aflatoxins.

▫ Too much fluid in the body's tissues, which

causes swelling under the skin (edema).
▫ Usually begins in the legs, but can involve the
whole body, including the face.
▫ Marked muscle atrophy
▫ Abdominal distension
▫ Round face
▫ Subcutaneous fat retention with loose inner
Protein Energy Malnutrition
inguinal skin folds
▫ Protein-energy undernutrition
▫ A condition arising from inadequate intake of
▫ Thin, dry, peeling skin with areas of scaling and
food rich in energy and protein, characterized by
hyperpigmentation
marked weight loss and failure to grow
▫ Dry, full, hypopigmented hair that falls out or is
▫ Kwashiorkor
easily plucked
▫ Marasmus
▫ Growth retardation
▫ Psychic changes (anorexia, apathy)
PEM in the Philippines
▫ Skin lesions/dermatitis (perineum, groin, limbs,
▫ For nearly thirty years, there have been almost
ears, armpits)
no improvements in the prevalence of
undernutrition in the Philippines.
Phenylketonuria
▫ PKU is caused by a change in the phenylalanine
▫ In September 2020, after seven months of
hydroxylase (PAH) gene.
community quarantine, 31% of families reported
▫ Phenylalanine hydroxylase breaksdown
experiencing hunger in the past 30 days, and 9%
phenylalanine
were suffering severe hunger.
▫ Phenylalanine can build up in the blood and
brain.
▫ Does not usually cause any symptoms if
Marasmus
treatment is started early.
Severe undernutrition — a deficiency in all the
▫ Without treatment, PKU can damage the
macronutrients that the body requires to function,
brain and nervous system, which can lead
including carbohydrates, protein and fats.
to learning disabilities.
▫ behavioral difficulties
Marasmus causes visible wasting of fat and
▫ frequent temper tantrums and episodes of
muscle under the skin, giving bodies an
self-harm
emaciated appearance.
▫ fairer skin, hair and eyes than siblings
▫ eczema
It causes stunted growth in children.
▫ jerking movements in arms and legs
▫ tremors
Kwashiorkor
▫ epilepsy
▫ Severe form of malnutrition
▫ musty smell to the breath, skin and urine
▫ Severe protein malnutrition
▫ Bilateral extremity swelling
▫ Usually affects infants and children.
▫ Poverty-stricken regions
▫ Diets based mainly on maize, cassava, or rice