# Oligopeptide > Mediated Wiki article. Canonical URL: https://mediated.wiki/source/Oligopeptide > Markdown URL: https://mediated.wiki/source/Oligopeptide.md > Source: https://en.wikipedia.org/wiki/Oligopeptide > Source revision: 1328272639 > License: Creative Commons Attribution-ShareAlike 4.0 International (https://creativecommons.org/licenses/by-sa/4.0/) Peptide consisting of two to twenty amino acids A tripeptide (example [Val](/source/Valine)-[Gly](/source/Glycine)-[Ala](/source/Alanine)) with **green** marked [amino end](/source/N-terminus) ([**L-Valine**](/source/Valine)) and **blue** marked [carboxyl end](/source/C-terminus) ([**L-Alanine**](/source/Alanine)) A tetrapeptide (example [Val](/source/Valine)-[Gly](/source/Glycine)-[Ser](/source/Serine)-[Ala](/source/Alanine)) with **green** marked [amino end](/source/N-terminus) ([**L-valine**](/source/Valine)) and **blue** marked [carboxyl end](/source/C-terminus) ([**L-alanine**](/source/Alanine)) An **oligopeptide** (*[oligo-](https://en.wiktionary.org/wiki/oligo-)*, "a few"), is a [peptide](/source/Peptide) consisting of two to twenty [amino acids](/source/Amino_acid), including [dipeptides](/source/Dipeptide), [tripeptides](/source/Tripeptide), [tetrapeptides](/source/Tetrapeptide), and other polypeptides. Some of the major classes of naturally occurring oligopeptides include [aeruginosins](/source/Aeruginosin), [cyanopeptolins](/source/Cyanopeptolin), [microcystins](/source/Microcystin), [microviridins](/source/Microviridin), [microginins](https://en.wikipedia.org/w/index.php?title=Microginin&action=edit&redlink=1), [anabaenopeptins](https://en.wikipedia.org/w/index.php?title=Anabaenopeptin&action=edit&redlink=1), and [cyclamides](/source/Cyclamide). Microcystins are best studied because of their potential toxicity impact in drinking water.[1] A review of some oligopeptides found that the largest class are the cyanopeptolins (40.1%), followed by microcystins (13.4%).[2] ## Production Oligopeptide classes are produced by [nonribosomal peptides](/source/Nonribosomal_peptide) synthases (NRPS), except cyclamides and microviridins are synthesized through [ribosomic](/source/Ribosome) pathways.[3] ## Examples Examples of oligopeptides include:[4] - [Amanitins](/source/Amanitins) - Cyclic peptides taken from carpophores of several different mushroom species. They are potent inhibitors of [RNA polymerases](/source/RNA_polymerase) in most eukaryotic species, the prevent the production of mRNA and protein synthesis. These peptides are important in the study of transcription. Alpha-amanitin is the main toxin from the species *[Amanita phalloides](/source/Amanita_phalloides)*, poisonous if ingested by humans or animals. - [Antipain](/source/Antipain) - An oligopeptide produced by various bacteria which acts as a [protease](/source/Protease) inhibitor. - [Ceruletide](/source/Ceruletide) - A specific decapeptide found in the skin of *Hyla caerulea*, the [Australian green tree frog](/source/Australian_Green_Tree_Frog). Ceruletide has very much in common with regard to action and composition to [cholecystokinin](/source/Cholecystokinin). It stimulates gastric, biliary, and pancreatic secretion; and certain [smooth muscle](/source/Smooth_muscle). It is used to induce [pancreatitis](/source/Pancreatitis) in experimental animal models. - [Glutathione](/source/Glutathione) - A tripeptide with many roles in cells. It conjugates to drugs to make them more soluble for excretion, is a cofactor for some enzymes, is involved in protein disulfide bond rearrangement and reduces peroxides. - [Leupeptins](/source/Leupeptin) - A group of acylated oligopeptides produced by Actinomycetes that function as protease inhibitors. They have been known to inhibit to varying degrees [trypsin](/source/Trypsin), [plasmin](/source/Plasmin), [kallikreins](/source/Kallikrein), [papain](/source/Papain) and the [cathepsins](/source/Cathepsin). - [Netropsin](/source/Netropsin) - A basic oligopeptide isolated from *[Streptomyces netropsis](/source/Streptomyces_netropsis)*. It is cytotoxic and its strong, specific binding to A-T areas of DNA is useful to genetics research. - [Pepstatins](/source/Pepstatin) - *N*-acylated oligopeptides isolated from culture filtrates of Actinomycetes, which act specifically to inhibit acid proteases such as pepsin and renin. - [Peptide T](/source/Peptide_T) - *N*-(*N*-(*N*(2)-(*N*-(*N*-(*N*-(*N*-D-Alanyl L-seryl)-L-threonyl)-L-threonyl) L-threonyl)-L-asparaginyl)-L-tyrosyl) L-threonine. Octapeptide sharing [sequence homology](/source/Sequence_homology) with HIV envelope protein gp120. It may be useful as antiviral agent in AIDS therapy. The core pentapeptide sequence, TTNYT, consisting of amino acids 4-8 in peptide T, is the HIV envelope sequence required for attachment to the CD4 receptor. - [Phalloidin](/source/Phalloidin) - A very toxic polypeptide isolated mainly from *[Amanita phalloides](/source/Amanita_phalloides)* (Agaricaceae) or death cap; causes fatal liver, kidney and CNS damage in mushroom poisoning; used in the study of liver damage. - [Teprotide](/source/Teprotide) - A human-made nonapeptide (Pyr-Trp-Pro-Arg-Pro-Gln-Ile-Pro-Pro) which is exactly the same as the peptide from the venom of the snake, Bothrops jararaca. It inhibits kininase II and angiotensin I and has been proposed as an antihypertensive agent. - [Tuftsin](/source/Tuftsin) - *N*(2)-((1-(*N*(2)-L-Threonyl)-L-lysyl)-L-prolyl)-L-arginine. A tetrapeptide manufactured in the spleen by enzymatic cleavage of a leukophilic gamma-globulin. It stimulates the phagocytic activity of blood polymorphonuclear leukocytes and neutrophils in particular. The peptide is located in the Fd fragment of the gamma-globulin molecule. ## See also - [Micropeptide](/source/Micropeptide) - [Oligoester](/source/Oligoester) - [Oligomer](/source/Oligomer) - [Oligopeptidase](/source/Oligopeptidase) - [Peptide synthesis](/source/Peptide_synthesis) - [Protease](/source/Protease) ## References 1. **[^](#cite_ref-1)** Martin Welker; Hans Von Döhren (2006). ["Cyanobacterial peptides – Nature's own combinatorial biosynthesis"](https://doi.org/10.1111%2Fj.1574-6976.2006.00022.x). *FEMS Microbiology Reviews*. **30** (4): 530–563. [doi](/source/Doi_(identifier)):[10.1111/j.1574-6976.2006.00022.x](https://doi.org/10.1111%2Fj.1574-6976.2006.00022.x). [PMID](/source/PMID_(identifier)) [16774586](https://pubmed.ncbi.nlm.nih.gov/16774586). 1. **[^](#cite_ref-2)** George E. Chlipala; Shunyan Mo; Jimmy Orjala (2011). ["Chemodiversity in Freshwater and Terrestrial Cyanobacteria – a Source for Drug Discovery"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3244969). *Curr Drug Targets*. **12** (11): 1654–73. [doi](/source/Doi_(identifier)):[10.2174/138945011798109455](https://doi.org/10.2174%2F138945011798109455). [PMC](/source/PMC_(identifier)) [3244969](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3244969). [PMID](/source/PMID_(identifier)) [21561419](https://pubmed.ncbi.nlm.nih.gov/21561419). 1. **[^](#cite_ref-3)** Ramsy Agha; Samuel Cirés; Lars Wörmer; Antonio Quesada (2013). ["Limited Stability of Microcystins in Oligopeptide Compositions of Microcystis aeruginosa (Cyanobacteria): Implications in the Definition of Chemotypes"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3717771). *Toxins*. **5** (6): 1089–1104. [doi](/source/Doi_(identifier)):[10.3390/toxins5061089](https://doi.org/10.3390%2Ftoxins5061089). [PMC](/source/PMC_(identifier)) [3717771](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3717771). [PMID](/source/PMID_(identifier)) [23744054](https://pubmed.ncbi.nlm.nih.gov/23744054). 1. **[^](#cite_ref-4)** Argos, Patrick. ["An Investigation of Oligopeptides Linking Domains in Protein Tertiary Structures and Possible Candidates for General Gene Fusion"](https://web.archive.org/web/20140728051840/http://download.bioon.com.cn/upload/month_0809/20080915_a342b2a65565db753bc8JmwXvbbtulIV.attach.pdf) (PDF). European Molecular Biology Laboratory. Archived from [the original](http://download.bioon.com.cn/upload/month_0809/20080915_a342b2a65565db753bc8JmwXvbbtulIV.attach.pdf) (PDF) on 28 July 2014. Retrieved 28 July 2014. ## External links Look up ***[oligopeptide](https://en.wiktionary.org/wiki/Special:Search/oligopeptide)*** in Wiktionary, the free dictionary. - [Structural Biochemistry/Proteins/Amino Acids](https://en.wikibooks.org/wiki/Structural_Biochemistry/Proteins/Amino_Acids) (Wikibooks) Authority control databases International GND National Czech Republic Other Yale LUX --- Adapted from the Wikipedia article [Oligopeptide](https://en.wikipedia.org/wiki/Oligopeptide) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/Oligopeptide?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.