Name: MENDOZA, JHUNLAINE KATE G.

ACTIVITY 3

AMINO ACIDS AND PEPTIDES

Introduction:

Among all the possible amino acids, only 20 are usually found in proteins. The general structures of
amino acids include an amino group and a carboxyl group, both of which are bonded to the alpha-
carbon (next to the carboxyl group). The alpha-carbon is also bonded to hydrogen and to the side chain
group, which is represented by the letter R. The R group determines the identity of the particular amino
acid. The three dimensional shape is known as its stereochemistry. ( Campbell & Farell, 2012)

Critical Thinking Questions

1. Differentiate between chiral and achiral.

-The mirror-image objects cannot be superimposed on another but are related to each other as
the right hand is to the left. Such nonsuperimposable mirror images are said to chiral. Achiral is
a term used to describe an object that is completely and identically superimposable with a
mirror object of itself. The nature of chirality is that generally, only simple molecules such as
hydrocarbons are likely to be achiral.

2. Differentiate between dextro and levo form.

- The terms dextrorotatory and levorotatory are useful when describing the rotation of plane-
polarized light by different chemical compounds. Dextrorotatory refers to the rotation of plane-
polarized light to the right side, whereas levorotatory refers to the rotation of plane-polarized
light to the left side. The process of this rotation of light is named as dextrorotation and
levorotation.

3. Differentiate between dextro-methorphan and levo-methorphan? Of dextro-cetirizine and levo-

cetirizine? Of dextro-ofloxacin and levo-ofloxacin (commonly, levofloxacin)?
- Dextromethorphan DXM has been widely used as a non-narcotic antitussive agent. DXM is a
safe drug available in many over-the-counter formulations and does not produce analgesic
effects in therapeutic dose; however, when exceeding label-specified maximum dosages, DXM
acts as a dissociative hallucinogen as a N-methyl-d-aspartate receptor antagonist . The
levorotatory enantiomer of DXM, levomethorphan LVM, is a potent analgesic and its use is
strictly controlled in the world as a narcotic drug

4. Why are amino acid side chains so important?

-A classification scheme for amino acids can be based on the properties of their side chains. Two
particularly important criteria are the polar and nonpolar nature of the side chain and the
presence of an acidic or basic group of the side chain.
 5. Differentiate between non-polar and polar amino acids in the tabular format. List down
examples

POLAR AMINO ACID VS NONPOLAR AMINO ACID

Polar amino acids are amino acids that have polarity. Nonpolar amino acids are amino acids that have no
polarity.

POLARITY

Polarity is present in polar amino acids. Polarity is absent in nonpolar amino acids.

HYDROPHOBICITY

Polar amino acids are hydrophilic. Nonpolar amino acids are hydrophobic.

EXAMPLES

Examples of polar amino acids include serine, lysine and Alanine, valine, leucine, isoleucine, phenylalanine,
aspartic acid. glycine, tryptophan, methionine, proline.
 6. Differentiate between an acid, a base and a neutral amino acid in a tabular format. List down
examples.

Acidic amino acid Neutral amino acid Basic amino acid

An amino acid with a second
acid meioty
Contain acidic side chains at the
neutral pH
Side chain contains carboxylic
groups (-COOH)
Consist of low pKa values, which
allow losing protons
Bear a negative charge in their
side chain
Include glutamic acid and
aspartic acid.
Amino acids that possess equal
number of carboxylic acid
groups and amino groups.
May be non-polar or polar.
The non-polar amino acids
contain alkyl groups as side
chains
The polar amino acids contain a
functional group.
The neutral amino acids can be
divided into two types:
Non-polar amino acids: These
amino acids contain an equal
number of carboxylic and amino
group along with an R group
which can be aliphatic or
aromatic.
An amino acid containing a
second basic group (usually an
amino group)
Contain basic side chains at the
neutral pH
Side chain contains amino
group (-NH2)
Consist of high pKa values,
which allow them to bind in
protons
Bear a positive charge in their
side chain
Lysine, arginine, and ornithine
are the three types.

Polar uncharged amino acids: In

this type of neutral amino acids,
the side chains contain
functional groups which possess
atoms like nitrogen, sulfur and
oxygen.
7. Differentiate between essential and non-essential amino acids. List down examples.

Essential amino acids Non-essential amino acids

The amino acids that cannot be synthesized The amino acids that can be synthesized\d by
by the human body are essential amino acids. the body are non-essential acids.

Must be obtained through the diet. Not necessary to obtain from diet.

Available in animal products. Available in both animal and plant products.

Examples are: phenylalanine, valine, Examples are: Alanine, arginine, cysteine,

threonine, tryptophan, isoleucine, histidine, tyrosine, glutamine, glutamate, glycine,
lysine, and leucine. histidine, serine, asparagine, aspartate, and
proline.

8. What is a peptide bond?

-Individual amino acids can be linked by forming covalent bonds. The bond is formed between
the carboxyl group of one amino acid and the amino group of the next one. Water is eliminated
in the process, and linked amino acid residues remain after water is eliminated. A bond formed
in this way is called a peptide bond.

9. Which groups on amino acids react to form a peptide bond?

-Peptides are formed by reacting the carboxyl group of one amino acid with the amino group of
another amino acid in covalent bond. Proteins consist of polypeptide chains; the number of
amino acids in a protein is usually 100 or more. The peptide group is planar; this stereochemical
constraint plays an important role in determining the three-dimensional structures of peptides
and proteins
10. Oxytocin and vasopressin are peptide hormones which are also use as drugs. What are the
functions of these drugs/ peptide hormones?
-Oxytocin has an isoleucine at position 3 and a leucine at position 8; it stimulates smooth muscle
contractions in the uterus during labor and in the mammary glands during lactation. While
vasopressin has a phenylalanine at position 3 and an arginine at position 8; it stimulates
resorption of water by the kidneys, thus raising blood pressure.

11. What is phenylketonuria?

- Phenylketonuria, also called PKU, is a rare inherited disorder that causes an amino acid called
phenylalanine to build up in the body. PKU is caused by a defect in the gene that helps create
the enzyme needed to break down phenylalanine.

12. Identify the nonpolar amino acid and the acidic amino acids in the following peptide:
Glu-Thr-Val- Asp- Ile- Ser- Ala
-In the peptide Glu-Thr-Val- Asp- Ile- Ser- Ala, the nonpolar amino acids are Val, Ile, and Ala; the
acidic amino acids are Glu and Asp.

13. Identify the polar amino acids, the aromatic amino acids, and the sulfur-containing amino acids,
given a peptide with the following acid sequence:

Val-Met- Ser- Ile- Phe- Arg- Cys- Tyr- Leu

Val- Valine
Met- Methionine
Ser- Serine
Ile- Isoleucine
Phe- Phenylalanine
Arg- Arginine
Cys- Cysteine
Tyr- Tyrosine
Leu- Leucine

14. What is an isoelectric point?

- The isoelectric point is the point at which the overall charge of the protein is zero (a neutral
charge). Separation of proteins at the isoelectric point is called isoelectric focusing.

15. What is a zwitterion?

-Zwitterions are compounds that have both positive and negative charge. It is usually considered
less likely to interfere with biochemical reactions than some of the earlier buffers.
16. Which would be better to eat before an exam, a glass of milk or a piece of cheese? Why?

-The tryptophan in milk might make your sleepy, whereas the tyramine in cheese should pep
you up

17. Suggest a reason why biosynthesis of amino acids and of protein would eventually cease in an
organism with carbohydrates as its only food source.
- Out of the 20 total amino acids in existence, 9 are considered "essential amino acids," which
cannot be made by the body. This means they must be consumed from food. The best sources
of these amino acids are from protein sources, specifically animal protein sources like meat,
eggs, and poultry. An organism that only eats carbohydrate-based foods may not consume
adequate amounts of all 9 essential amino acids, which would eventually lead to an inability to
synthesize proteins in the body.

18. Why might a glass of warm milk help you sleep at night?
-The high concentration of tryptophan in milk protein may mildly elevate level of serotonin,
which relaxes the brain.

19. What is a monoamine oxidase, and what function does it serve?

-A monoamine oxidase is an enzyme that degrades compounds with an amino group, including
nuerotansmitters; consequently, it can control a person’s mental state.

20. Give example of drugs that are monoamine oxidase (MAO) inhibitors.
- Isocarboxazid (Marplan)
-Phenelzine (Nardil)
-Selegiline (Emsam)
-Tranylcypromine (Parnate)

21. Which amino acids or their derivatives are neurotransmitters?

-Tyrosine, tryptophan and their derivatives are neurotransmitters.

22. Consider the peptides Ser-Glu-Gly-His-Ala and Gly-His-Ala-Glu-Ser. How do these two peptides
differ?
- Ser-Glu-Gly-His-Ala and Gly-His-Ala-Glu-Ser peptides differ in amino acid sequences but not in
composition

23. What is an enkephalin?

- Enkephalin, naturally occurring peptide that has potent painkilling effects and is released by
neurons in the central nervous system and by cells in the adrenal medulla.
24. What drugs affect enkephalin?
-Psychostimulant drugs, like amphetamine and cocaine, significantly increase the content of
enkephalin in these brain structures.

25. What is dopamine? What amino acid was it derived from?

- Dopamine is a type of neurotransmitter. Your body makes it, and your nervous system uses it
to send messages between nerve cells. That's why it's sometimes called a chemical messenger.
Dopamine plays a role in how we feel pleasure. It's a big part of our unique human ability to
think and plan. Dopamine is a derivative of the amino acid tyrosine. Tyrosine is modified by
tyrosine hydroxylase to form DOPA, and the dopamine

26. What drugs contain dopamine? What is its therapeutic use?

-Dopamine has many functions outside the brain. It acts as a vasodilator, helping to widen blood
vessels. It helps to increase urine output in the kidneys, and in the pancreas, it reduces the
production of insulin, a hormone involved in blood sugar regulation.

-There are a few classes of medication that work on the dopamine pathways of the brain to
treat disease. They include: Levodopa (L-dopa), Mirapex (ramipexole), Neupro (rotigotine) and
Requip (ropinirole)

27. What is 5-hydroxytryptamine? What amino acid was it derived from?

-A hormone found in the brain, platelets, digestive tract, and pineal gland. It acts both as a
neurotransmitter-a substance that nerves use to send messages to one another) and a
vasoconstrictor -a substance that causes blood vessels to narrow. 5-hydroxytryptamine (5-HT) is
derived from the essential amino acid L-tryptophan.

28. How do the oxidized and reduced forms of glutathione differ from each other?
-The reduced form of glutathione consists of three amino acids with sulfhydryl group; the
oxidized form consists of six amino acids and can be considered the result of linking two
molecules of reduced glutathione by a disulfide bridge.