peptides

Ribosomal peptides
Are synthesized by translation of mRNA. They are often subjected to proteolysis to generate the mature form. These function, typically in higher organisms, as hormones and signaling molecules. Some organisms produce peptides as antibiotics, such as microcins.[1] Since they are translated, the amino acid residues involved are restricted to those utilized by the ribosome. However, these peptides frequently have posttranslational modifications, such as phosphorylation, hydroxylation, sulfonation, palmitylation, glycosylation and disulfide formation. In general, they are linear, although lariat structures have been observed.[2] More exotic manipulations do occur, such as racemization of L-amino acids to D-amino acids in platypus venom.[3]
Nonribosomal peptides
These peptides are assembled by enzymes that are specific to each peptide, rather than by the ribosome. The most common non-ribosomal peptide is glutathione, which is a component of the antioxidant defenses of most aerobic organisms.[4] Other nonribosomal peptides are most common in unicellular organisms, plants, and fungi and are synthesized by modular enzyme complexes called nonribosomal peptide synthetases.[5] 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.[6] 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. Oxazoles, thiazoles often indicate that the compound was synthesized in this fashion.[7]
Peptones
See also Tryptone
Are derived from animal milk or meat digested by proteolytic digestion. In addition to containing small peptides, the resulting spray-dried material includes fats, metals, salts, vitamins and many other biological compounds. Peptone is used in nutrient media for growing bacteria and fungi.[8]
Peptide Fragments
Refer to fragments of proteins that are used to identify or quantify the source protein.[9] Often these are the products of enzymatic degradation performed in the laboratory on a controlled sample, but can also be forensic or paleontological samples which have been degraded by natural effects.[10][11]

[edit] Peptides in molecular biology
Peptides have received prominence in molecular biology in recent times for several reasons. The first and most important is that peptides allow the creation of peptide antibodies in animals without the need to purify the protein of interest.[12] This involves synthesizing antigenic peptides of sections of the protein of interest. These will then be used to make antibodies in a rabbit or mouse against the protein.
Another reason is that peptides have become instrumental in mass spectrometry, allowing the identification of proteins of interest based on peptide masses and sequence. In this case the peptides are most often generated by in-gel digestion after electrophoretic separation of the proteins.
Peptides have recently been used in the study of protein structure and function. For example, synthetic peptides can be used as probes to see where protein-peptide interactions occur.
Inhibitory peptides are also used in clinical research to examine the effects of peptides on the inhibition of cancer proteins and other diseases.

[edit] Well-known peptide families in humans
The peptide families in this section are all 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 signalling functions.

[edit] The Tachykinin peptides
Substance P
Kassinin
Neurokinin A
Eledoisin
Neurokinin B

[edit] Vasoactive intestinal peptides
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

[edit] Pancreatic polypeptide-related peptides
NPY
PYY (Peptide YY)
APP (Avian Pancreatic Polypeptide)
PPY Pancreatic PolYpeptide

[edit] Opioid peptides
Proopiomelanocortin (POMC) peptides
Enkephalin pentapeptides
Prodynorphin peptides

[edit] Calcitonin peptides
Calcitonin
Amylin
AGG01

[edit] Other peptides
B-type Natriuretic Peptide (BNP) - produced in myocardium & useful in medical diagnosis

[edit] Notes on terminology
A polypeptide is a single linear chain of amino acids.
A protein is one or more polypeptides more than about 50 amino acids long.
An oligopeptide or (simply) a peptide is a polypeptide less than 30-50 amino acids long.
A dipeptide has two amino acids.
A tripeptide has three amino acids.
A pentapeptide has five amino acids.
An octapeptide has eight amino acids. (e.g., angiotensin II.
A nonapeptide has nine amino acids (e.g., oxytocin).
A decapeptide has ten amino acids (e.g., gonadotropin-releasing hormone & angotensin I).
A neuropeptide is a peptide that is active in association with neural tissue.
A peptide hormone is a peptide that acts as a hormone.

[edit] See also
Peptidomimetics (such as peptoids and β-peptides) to peptides, but with different properties.
bis-peptide
Peptide synthesis
Translation
Ribosome
Argireline

[edit] References
^ Duquesne S, Destoumieux-Garzón D, Peduzzi J, Rebuffat S (2007). "Microcins, gene-encoded antibacterial peptides from enterobacteria". Natural product reports 24 (4): 708–34. doi:10.1039/b516237h. PMID 17653356.
^ Pons M, Feliz M, Antònia Molins M, Giralt E (1991). "Conformational analysis of bacitracin A, a naturally occurring lariat". Biopolymers 31 (6): 605–12. doi:10.1002/bip.360310604. PMID 1932561.
^ Torres AM, Menz I, Alewood PF, et al (2002). "D-Amino acid residue in the C-type natriuretic peptide from the venom of the mammal, Ornithorhynchus anatinus, the Australian platypus". FEBS Lett. 524 (1-3): 172–6. doi:10.1016/S0014-5793(02)03050-8. PMID 12135762.
^ Meister A, Anderson M (1983). "Glutathione". Annu Rev Biochem 52: 711 – 60. doi:10.1146/annurev.bi.52.070183.003431. PMID 6137189.
^ Hahn M, Stachelhaus T (2004). "Selective interaction between nonribosomal peptide synthetases is facilitated by short communication-mediating domains". Proc. Natl. Acad. Sci. U.S.A. 101 (44): 15585–90. doi:10.1073/pnas.0404932101. PMID 15498872.
^ Finking R, Marahiel MA (2004). "Biosynthesis of nonribosomal peptides1". Annu. Rev. Microbiol. 58: 453–88. doi:10.1146/annurev.micro.58.030603.123615. PMID 15487945.
^ Du L, Shen B (2001). "Biosynthesis of hybrid peptide-polyketide natural products". Current opinion in drug discovery & development 4 (2): 215–28. PMID 11378961.
^ Payne JW (1976). "Peptides and micro-organisms". Adv. Microb. Physiol. 13: 55–113. PMID 775944.
^ Hummel J, Niemann M, Wienkoop S, et al (2007). "ProMEX: a mass spectral reference database for proteins and protein phosphorylation sites". BMC Bioinformatics 8: 216. doi:10.1186/1471-2105-8-216. PMID 17587460.
^ Webster J, Oxley D (2005). "Peptide mass fingerprinting: protein identification using MALDI-TOF mass spectrometry". Methods Mol. Biol. 310: 227–40. PMID 16350956.
^ Marquet P, Lachâtre G (1999). "Liquid chromatography-mass spectrometry: potential in forensic and clinical toxicology". J. Chromatogr. B Biomed. Sci. Appl. 733 (1-2): 93–118. doi:10.1016/S0378-4347(99)00147-4. PMID 10572976.