# Antipain

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This article is about the protease inhbitor. For the article about pain relief, see [analgesic](/source/Analgesic).

Antipain Names IUPAC name N2-{[(1S)-1-carboxy-2-phenylethyl]carbamoyl}-N5-(diaminomethylidene)-L-ornithyl-N-{(2S)-5-[(diaminomethylidene)amino]-1-oxopentan-2-yl}-L-valinamide Identifiers CAS Number 37691-11-5 N 3D model (JSmol) Interactive image ChemSpider 34678 Y ECHA InfoCard 100.048.738 PubChem CID 37817 UNII 47V479BE6L N CompTox Dashboard (EPA) DTXSID40958733 InChI InChI=1S/C27H44N10O6/c1-16(2)21(23(40)34-18(15-38)10-6-12-32-25(28)29)37-22(39)19(11-7-13-33-26(30)31)35-27(43)36-20(24(41)42)14-17-8-4-3-5-9-17/h3-5,8-9,15-16,18-21H,6-7,10-14H2,1-2H3,(H,34,40)(H,37,39)(H,41,42)(H4,28,29,32)(H4,30,31,33)(H2,35,36,43)/t18-,19-,20-,21-/m0/s1 Y Key: SDNYTAYICBFYFH-TUFLPTIASA-N Y InChI=1/C27H44N10O6/c1-16(2)21(23(40)34-18(15-38)10-6-12-32-25(28)29)37-22(39)19(11-7-13-33-26(30)31)35-27(43)36-20(24(41)42)14-17-8-4-3-5-9-17/h3-5,8-9,15-16,18-21H,6-7,10-14H2,1-2H3,(H,34,40)(H,37,39)(H,41,42)(H4,28,29,32)(H4,30,31,33)(H2,35,36,43)/t18-,19-,20-,21-/m0/s1 Key: SDNYTAYICBFYFH-TUFLPTIABE SMILES O=C[C@@H](NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)N[C@H](C(=O)O)Cc1ccccc1)CCC/N=C(\N)N)C(C)C)CCC/N=C(\N)N Properties Chemical formula C27H44N10O6 Molar mass 604.713 g·mol−1 Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa). N verify (what is YN ?) Infobox references

Chemical compound

**Antipain** is an [oligopeptide](/source/Oligopeptide) that is isolated from [actinomycetes](/source/Actinomycetes) and used in biochemical research as a [protease inhibitor](/source/Protease_inhibitor_(biology)) of [trypsin](/source/Trypsin) and [papain](/source/Papain).[1] It was discovered in 1972 and was the first natural peptide found that contained an [ureylene](/source/Ureylene) group.[2] Antipain can aid in prevention of [coagulation](/source/Coagulation) in blood. It is an inhibitor of serine and cysteine proteases.[3]

It has been crystallized in complexes with [carboxypeptidase](/source/Carboxypeptidase), which is obtained from [wheat](/source/Wheat),[4] and *[Leishmania major](/source/Leishmania_major)* [oligopeptidase](/source/Oligopeptidase) B.[5] In both cases, the backbone carbonyl of the terminal [arginine](/source/Arginine) of antipain forms a covalent bond to the active site [serine](/source/Serine) in the protease.

A study was performed for information on the effect of antipain on the quality of post-thawed ram [semen](/source/Semen).[6] The results from this experiment concluded that antipain aided in the quality of ram semen by maintaining the sperm mobility.[6] Antipain includes the function to inhibit a degrading enzyme, called [plasmin](/source/Plasmin), permitting this substance to be able to improve the resistance of membrane disruption by freezing temperatures.[6]

Antipain Y, a similar chemical compound that is an [analog](/source/Analog_(chemistry)) of antipain, which was isolated from a species of *[Streptomyces](/source/Streptomyces)*, inhibits the release of neurotransmitters in rat dorsal root ganglion neurons.[7]

## References

1. **[^](#cite_ref-1)** Suda H, Aoyagi T, Hamada M, Takeuchi T, Umezawa H (April 1972). ["Antipain, a new protease inhibitor isolated from actinomycetes"](https://doi.org/10.7164%2Fantibiotics.25.263). *The Journal of Antibiotics*. **25** (4): 263–266. [doi](/source/Doi_(identifier)):[10.7164/antibiotics.25.263](https://doi.org/10.7164%2Fantibiotics.25.263). [PMID](/source/PMID_(identifier)) [4559651](https://pubmed.ncbi.nlm.nih.gov/4559651).

1. **[^](#cite_ref-2)** Umezawa S, Tatsuta K, Fujimoto K, Tsuchiya T, Umezawa H (April 1972). ["Structure of antipain, a new Sakaguchi-positive product of streptomyces"](https://doi.org/10.7164%2Fantibiotics.25.267). *The Journal of Antibiotics*. **25** (4): 267–270. [doi](/source/Doi_(identifier)):[10.7164/antibiotics.25.267](https://doi.org/10.7164%2Fantibiotics.25.267). [PMID](/source/PMID_(identifier)) [5052959](https://pubmed.ncbi.nlm.nih.gov/5052959).

1. **[^](#cite_ref-3)** Lackie J (2012). *A Dictionary of Biomedicine*. Oxford University Press. [ISBN](/source/ISBN_(identifier)) [9780199549351](https://en.wikipedia.org/wiki/Special:BookSources/9780199549351).

1. **[^](#cite_ref-4)** PDB ENTRY [1bcr](https://www.ebi.ac.uk/pdbe/entry/pdb/1bcr) Bullock TL, Breddam K, Remington SJ (February 1996). "Peptide aldehyde complexes with wheat serine carboxypeptidase II: implications for the catalytic mechanism and substrate specificity". *Journal of Molecular Biology*. **255** (5): 714–725. [doi](/source/Doi_(identifier)):[10.1006/jmbi.1996.0058](https://doi.org/10.1006%2Fjmbi.1996.0058). [PMID](/source/PMID_(identifier)) [8636973](https://pubmed.ncbi.nlm.nih.gov/8636973).

1. **[^](#cite_ref-5)** PDB ENTRY [2xe4](https://www.ebi.ac.uk/pdbe/entry/pdb/2xe4) McLuskey K, Paterson NG, Bland ND, Isaacs NW, Mottram JC (December 2010). ["Crystal structure of Leishmania major oligopeptidase B gives insight into the enzymatic properties of a trypanosomatid virulence factor"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2998157). *The Journal of Biological Chemistry*. **285** (50): 39249–39259. [doi](/source/Doi_(identifier)):[10.1074/jbc.M110.156679](https://doi.org/10.1074%2Fjbc.M110.156679). [PMC](/source/PMC_(identifier)) [2998157](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2998157). [PMID](/source/PMID_(identifier)) [20926390](https://pubmed.ncbi.nlm.nih.gov/20926390).

1. ^ [***a***](#cite_ref-Akhtarshenas_6-0) [***b***](#cite_ref-Akhtarshenas_6-1) [***c***](#cite_ref-Akhtarshenas_6-2) Akhtarshenas, Bahareh; Karami Shabankareh, Hamed; Hajarian, Hadi; Bucak, Mustafa Numan; Abdolmohammadi, Ali Reza; Dashtizad, Mojtaba (2018). "The protease inhibitor antipain has a beneficial synergistic effect with trehalose for ram semen cryopreservation". *Reproduction in Domestic Animals*. **53** (6): 1359–1366. [doi](/source/Doi_(identifier)):[10.1111/rda.13253](https://doi.org/10.1111%2Frda.13253). [PMID](/source/PMID_(identifier)) [30011087](https://pubmed.ncbi.nlm.nih.gov/30011087). [S2CID](/source/S2CID_(identifier)) [51629940](https://api.semanticscholar.org/CorpusID:51629940).

1. **[^](#cite_ref-7)** Nakae K, Kojima F, Sawa R, Kubota Y, Igarashi M, Kinoshita N, et al. (January 2010). ["Antipain Y, a new antipain analog that inhibits neurotransmitter release from rat dorsal root ganglion neurons"](https://doi.org/10.1038%2Fja.2009.109). *The Journal of Antibiotics*. **63** (1): 41–44. [doi](/source/Doi_(identifier)):[10.1038/ja.2009.109](https://doi.org/10.1038%2Fja.2009.109). [PMID](/source/PMID_(identifier)) [19911027](https://pubmed.ncbi.nlm.nih.gov/19911027).

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Adapted from the Wikipedia article [Antipain](https://en.wikipedia.org/wiki/Antipain) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/Antipain?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.