A 

tetrapeptide (example Val-Gly-Ser-Ala) with greenmarked amino end (L-Valine) and 

blue marked carboxyl end (L-Alanine).
Peptides (from Ancient Greek πεπτός (peptós) 'digested', from πέσσειν (péssein) 'to digest') are
short chains of amino acids linked by peptide bonds.[1][2] Chains of fewer than twenty amino acids
are called oligopeptides, and include dipeptides, tripeptides, and tetrapeptides.
A polypeptide is a longer, continuous, unbranched peptide chain.[3] Hence, peptides fall under
the broad chemical classes of biological polymers and oligomers, alongside nucleic
acids, oligosaccharides, polysaccharides, and others.
A polypeptide that contains more than approximately fifty amino acids is known as a protein.[3][4]
[5]
 Proteins consist of one or more polypeptides arranged in a biologically functional way, often
bound to ligands such as coenzymes and cofactors, or to another protein or
other macromolecule such as DNA or RNA, or to complex macromolecular assemblies.[6]
Amino acids that have been incorporated into peptides are termed residues. A water molecule is
released during formation of each amide bond.[7] All peptides except cyclic peptides have an N-
terminal (amine group) and C-terminal (carboxyl group) residue at the end of the peptide (as
shown for the tetrapeptide in the image).

Contents

 1Classes

 2Chemical synthesis

 3Example families

o 3.1Antimicrobial peptides

o 3.2Tachykinin peptides

o 3.3Vasoactive intestinal peptides

o 3.4Pancreatic polypeptide-related peptides

o 3.5Opioid peptides

o 3.6Calcitonin peptides

o 3.7Self-Assembling peptides

o 3.8Other peptides

 4Terminology

o 4.1Length
 o 4.2Number of amino acids

o 4.3Function

 5See also

 6References

Classes[edit]
Many kinds of peptides are known. They have been classified or categorized according to their
sources and functions. According to the Handbook of Biologically Active Peptides, some groups
of peptides include plant peptides, bacterial/antibiotic peptides, fungal peptides, invertebrate
peptides, amphibian/skin peptides, venom peptides, cancer/anticancer peptides, vaccine
peptides, immune/inflammatory peptides, brain peptides, endocrine peptides, ingestive peptides,
gastrointestinal peptides, cardiovascular peptides, renal peptides, respiratory peptides, opiate
peptides, neurotrophic peptides, and blood–brain peptides.[8]
Some ribosomal peptides are subject to proteolysis. These function, typically in higher
organisms, as hormones and signaling molecules. Some microbes produce peptides
as antibiotics, such as microcins and bacteriocins.[9]
Peptides frequently have post-translational modifications such
as phosphorylation, hydroxylation, sulfonation, palmitoylation, glycosylation,
and disulfide formation. In general, peptides are linear, although lariat structures have been
observed.[10] More exotic manipulations do occur, such as racemization of L-amino acids to D-
amino acids in platypus venom.[11]
Nonribosomal peptides are assembled by enzymes, not the ribosome. A common non-ribosomal
peptide is glutathione, a component of the antioxidant defenses of most aerobic organisms.
[12]
 Other nonribosomal peptides are most common in unicellular organisms, plants, and fungi and
are synthesized by modular enzyme complexes called nonribosomal peptide synthetases.[13]
These complexes are often laid out in a similar fashion, and they can contain many different
modules to perform a diverse set of chemical manipulations on the developing product.[14] These
peptides are often cyclic and can have highly complex cyclic structures, although linear
nonribosomal peptides are also common. Since the system is closely related to the machinery for
building fatty acids and polyketides, hybrid compounds are often found. The presence
of oxazoles or thiazoles often indicates that the compound was synthesized in this fashion.[15]
Peptones are derived from animal milk or meat digested by proteolysis.[16] In addition to
containing small peptides, the resulting material includes fats, metals, salts, vitamins, and many
other biological compounds. Peptones are used in nutrient media for growing bacteria and fungi.
[17]

Peptide fragments refer to fragments of proteins that are used to identify or quantify the source
protein.[18] Often these are the products of enzymatic degradation performed in the laboratory on
a controlled sample, but can also be forensic or paleontological samples that have been
degraded by natural effects.[19][20]

Chemical synthesis[edit]
Main article: Peptide synthesis
Solid-phase peptide synthesis on a rink amide resin using Fmoc-α-amine-protected amino acid

Example families[edit]
The peptide families in this section are ribosomal peptides, usually with hormonal activity. All of
these peptides are synthesized by cells as longer "propeptides" or "proproteins" and truncated
prior to exiting the cell. They are released into the bloodstream where they perform their
signaling functions.

Antimicrobial peptides[edit]
 Magainin family
 Cecropin family
 Cathelicidin family
 Defensin family
Tachykinin peptides[edit]
Main article: Tachykinin peptides

 Substance P
 Kassinin
 Neurokinin A
 Eledoisin
 Neurokinin B
Vasoactive intestinal peptides[edit]
Main article: Secretin family

 VIP (Vasoactive Intestinal Peptide; PHM27)
 PACAP Pituitary Adenylate Cyclase Activating Peptide
 Peptide PHI 27 (Peptide Histidine Isoleucine 27)
 GHRH 1-24 (Growth Hormone Releasing Hormone 1-24)
 Glucagon
 Secretin
Pancreatic polypeptide-related peptides[edit]
 NPY (NeuroPeptide Y)
 PYY (Peptide YY)
  APP (Avian Pancreatic Polypeptide)
 PPY Pancreatic PolYpeptide
Opioid peptides[edit]
Main article: Opioid peptide

 Proopiomelanocortin (POMC) peptides
 Enkephalin pentapeptides
 Prodynorphin peptides
Calcitonin peptides[edit]
 Calcitonin
 Amylin
 AGG01
Self-Assembling peptides[edit]
 Aromatic short peptides[21][22]
 Biomimetic peptides[23]
 Peptide amphiphiles[24][25][26][27]
 Peptide dendrimers[28]
Other peptides[edit]
 B-type Natriuretic Peptide (BNP) - produced in the myocardium and useful in medical
diagnosis
 Lactotripeptides - Lactotripeptides might reduce blood pressure,[29][30][31] although the
evidence is mixed.[32]
 Peptidic components from traditional Chinese medicine Colla Corii Asini in
hematopoiesis.[33]