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Peptide

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A tetrapeptide (example Val-Gly-Ser-Ala) with green marked amino end (L-Valine) and
blue marked carboxyl end (L-Alanine).

Peptides (from Greek language πεπτός, peptós "digested"; derived from πέσσειν, péssein "to digest") are short chains of amino acids linked by peptide (amide) bonds.[1] The simplest peptides are dipeptides, followed by tripeptides, tetrapeptides, etc. A polypeptide is a long, continuous, and unbranched peptide chain. Hence, peptides fall under the broad chemical classes of biological oligomers and polymers, alongside nucleic acids, oligosaccharides and polysaccharides, etc.

Peptides are distinguished from proteins on the basis of size, and as an arbitrary benchmark can be understood to contain approximately 50 or fewer amino acids.[2][3] 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 (DNA, RNA, etc.), or to complex macromolecular assemblies.[4] Finally, while aspects of the lab techniques applied to peptides versus polypeptides and proteins differ (e.g., the specifics of electrophoresis, chromatography, etc.), the size boundaries that distinguish peptides from polypeptides and proteins are not absolute: long peptides such as amyloid beta have been referred to as proteins, and smaller proteins like insulin have been considered peptides.

Amino acids that have been incorporated into peptides are termed "residues". A water molecule is released during formation of each amide bond.[5] 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).

ClassesEdit

Many kinds of peptides are known. They have been classified or categorized according to their sources and function. 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.[6]

Some ribosomal peptides are subject to proteolysis. These function, typically in higher organisms, as hormones and signaling molecules. Some organisms produce peptides as antibiotics, such as microcins.[7]

Peptides frequently have posttranslational modifications such as phosphorylation, hydroxylation, sulfonation, palmitoylation, glycosylation and disulfide formation. In general, peptides are linear, although lariat structures have been observed.[8] More exotic manipulations do occur, such as racemization of L-amino acids to D-amino acids in platypus venom.[9]

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.[10] Other nonribosomal peptides are most common in unicellular organisms, plants, and fungi and are synthesized by modular enzyme complexes called nonribosomal peptide synthetases.[11]

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.[12] 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.[13]

Peptide fragments refer to fragments of proteins that are used to identify or quantify the source protein.[14] 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.[15][16]

Chemical synthesisEdit

 
Solid-phase peptide synthesis on a rink amide resin using Fmoc-α-amine-protected amino acid

Example familiesEdit

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 peptidesEdit

Tachykinin peptidesEdit

Vasoactive intestinal peptidesEdit

  • 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 peptidesEdit

  • NPY (NeuroPeptide Y)
  • PYY (Peptide YY)
  • APP (Avian Pancreatic Polypeptide)
  • PPY Pancreatic PolYpeptide

Opioid peptidesEdit

Calcitonin peptidesEdit

Self-Assembling peptidesEdit

Other peptidesEdit

TerminologyEdit

LengthEdit

Several terms related to peptides have no strict length definitions, and there is often overlap in their usage.

  • A polypeptide is a single linear chain of many amino acids (any length), held together by amide bonds.
  • A protein consists of one or more polypeptides (more than about 50 amino acids long).
  • An oligopeptide consists of only a few amino acids (between two and twenty).
 
A tripeptide (example Val-Gly-Ala) with
green marked amino end (L-Valine) and
blue marked carboxyl end (L-Alanine)

Number of amino acidsEdit

Peptides of defined length are named using IUPAC numerical multiplier prefixes.

FunctionEdit

  • A neuropeptide is a peptide that is active in association with neural tissue.
  • A lipopeptide is a peptide that has a lipid connected to it, and pepducins are lipopeptides that interact with GPCRs.
  • A peptide hormone is a peptide that acts as a hormone.
  • A proteose is a mixture of peptides produced by the hydrolysis of proteins. The term is somewhat archaic.
  • A peptidergic agent (or drug) is a chemical which functions to directly modulate the peptide systems in the body or brain. An example is opioidergics, which are neuropeptidergics.

See alsoEdit

ReferencesEdit

  1. ^ Nelson, David L.; Cox, Michael M. (2005), Principles of Biochemistry (4th ed.), New York: W. H. Freeman, ISBN 0-7167-4339-6
  2. ^ IUPAC, Compendium of Chemical Terminology, 2nd ed. (the "Gold Book") (1997). Online corrected version:  (2006–) "proteins". doi:10.1351/goldbook.P04898
  3. ^ "What are peptides". Zealand Pharma A/S. Archived from the original on 2014-07-14.
  4. ^ Ardejani, Maziar S.; Orner, Brendan P. (2013-05-03). "Obey the Peptide Assembly Rules". Science. 340 (6132): 561–562. Bibcode:2013Sci...340..561A. doi:10.1126/science.1237708. ISSN 0036-8075. PMID 23641105.
  5. ^ IUPAC, Compendium of Chemical Terminology, 2nd ed. (the "Gold Book") (1997). Online corrected version:  (2006–) "amino-acid residue in a polypeptide". doi:10.1351/goldbook.A00279
  6. ^ Abba J. Kastin, ed. (2013). Handbook of Biologically Active Peptides (2nd ed.). ISBN 978-0-12-385095-9.
  7. ^ Duquesne S, Destoumieux-Garzón D, Peduzzi J, Rebuffat S (August 2007). "Microcins, gene-encoded antibacterial peptides from enterobacteria". Natural Product Reports. 24 (4): 708–34. doi:10.1039/b516237h. PMID 17653356.
  8. ^ Pons M, Feliz M, Antònia Molins M, Giralt E (May 1991). "Conformational analysis of bacitracin A, a naturally occurring lariat". Biopolymers. 31 (6): 605–12. doi:10.1002/bip.360310604. PMID 1932561.
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  10. ^ Meister A, Anderson ME; Anderson (1983). "Glutathione". Annual Review of Biochemistry. 52 (1): 711–60. doi:10.1146/annurev.bi.52.070183.003431. PMID 6137189.
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