Antipain: Difference between revisions

{{about|the protease inhbitor|the article about pain relief|analgesic}}

| Verifiedfields = changed

| Watchedfields = changed

| verifiedrevid = 457811721

|Section1={{Chembox Identifiers

| CASNo = 37691-11-5

| CASNo_Ref = {{cascite|changed|??}}

| PubChem = 37817

| ChemSpiderID_Ref = {{chemspidercite|correct|chemspider}}

| ChemSpiderID = 34678

| UNII_Ref = {{fdacite|changed|FDA}}

| UNII = 47V479BE6L

| 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

| 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

| InChIKey = SDNYTAYICBFYFH-TUFLPTIABE

| StdInChI_Ref = {{stdinchicite|correct|chemspider}}

| StdInChI = 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

| StdInChIKey_Ref = {{stdinchicite|correct|chemspider}}

| StdInChIKey = SDNYTAYICBFYFH-TUFLPTIASA-N

|Section2={{Chembox Properties

| C=27 | H=44 | N=10 | O=6

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|Section3={{Chembox Hazards

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'''Antipain''' is an [[oligopeptide]] that is isolated from [[actinomycetes]] and used in biochemical research as a [[Protease inhibitor (biology)|protease inhibitor]] of [[trypsin]] and [[papain]].<ref>{{cite journal | vauthors = Suda H, Aoyagi T, Hamada M, Takeuchi T, Umezawa H | title = Antipain, a new protease inhibitor isolated from actinomycetes | journal = The Journal of Antibiotics | volume = 25 | issue = 4 | pages = 263–266 | date = April 1972 | pmid = 4559651 | doi = 10.7164/antibiotics.25.263 | doi-access = free }}</ref> It was discovered in 1972 and was the first natural peptide found that contained an [[ureylene]] group.<ref>{{cite journal | vauthors = Umezawa S, Tatsuta K, Fujimoto K, Tsuchiya T, Umezawa H | title = Structure of antipain, a new Sakaguchi-positive product of streptomyces | journal = The Journal of Antibiotics | volume = 25 | issue = 4 | pages = 267–270 | date = April 1972 | pmid = 5052959 | doi = 10.7164/antibiotics.25.267 | doi-access = free }}</ref> Antipain can aid in prevention of [[coagulation]] in blood. It is an inhibitor of serine and cysteine proteases.<ref>{{Cite book| vauthors = Lackie J |title=A Dictionary of Biomedicine|publisher=Oxford University Press|year=2012|isbn=9780199549351}}</ref>

It has been crystallized in complexes with [[carboxypeptidase]], which is obtained from [[wheat]],<ref>PDB ENTRY {{PDBe|1bcr}} {{cite journal | vauthors = Bullock TL, Breddam K, Remington SJ | title = Peptide aldehyde complexes with wheat serine carboxypeptidase II: implications for the catalytic mechanism and substrate specificity | journal = Journal of Molecular Biology | volume = 255 | issue = 5 | pages = 714–725 | date = February 1996 | pmid = 8636973 | doi = 10.1006/jmbi.1996.0058 }}</ref> and ''[[Leishmania major]]'' [[oligopeptidase]] B.<ref>PDB ENTRY {{PDBe|2xe4}} {{cite journal | vauthors = McLuskey K, Paterson NG, Bland ND, Isaacs NW, Mottram JC | title = Crystal structure of Leishmania major oligopeptidase B gives insight into the enzymatic properties of a trypanosomatid virulence factor | journal = The Journal of Biological Chemistry | volume = 285 | issue = 50 | pages = 39249–39259 | date = December 2010 | pmid = 20926390 | pmc = 2998157 | doi = 10.1074/jbc.M110.156679 | doi-access = free }}</ref> In both cases, the backbone carbonyl of the terminal [[arginine]] of antipain forms a covalent bond to the active site [[serine]] in the protease.

A study was performed for information on the effect of antipain on the quality of post-thawed ram [[semen]].<ref name=Akhtarshenas>{{Cite journal | doi = 10.1111/rda.13253 | title = The protease inhibitor antipain has a beneficial synergistic effect with trehalose for ram semen cryopreservation | date = 2018 | last1 = Akhtarshenas | first1 = Bahareh | last2 = Karami Shabankareh | first2 = Hamed | last3 = Hajarian | first3 = Hadi | last4 = Bucak | first4 = Mustafa Numan | last5 = Abdolmohammadi | first5 = Ali Reza | last6 = Dashtizad | first6 = Mojtaba | journal = Reproduction in Domestic Animals | volume = 53 | issue = 6 | pages = 1359–1366 | pmid = 30011087 | s2cid = 51629940 }}</ref> The results from this experiment concluded that antipain aided in the quality of ram semen by maintaining the sperm mobility.<ref name=Akhtarshenas/> Antipain includes the function to inhibit a degrading enzyme, called [[plasmin]], permitting this substance to be able to improve the resistance of membrane disruption by freezing temperatures.<ref name=Akhtarshenas/>

Antipain Y, a similar chemical compound that is an [[analog (chemistry)|analog]] of antipain, which was isolated from a species of ''[[Streptomyces]]'', inhibits the release of neurotransmitters in rat dorsal root ganglion neurons.<ref>{{cite journal | vauthors = Nakae K, Kojima F, Sawa R, Kubota Y, Igarashi M, Kinoshita N, Adachi H, Nishimura Y, Akamatsu Y | display-authors = 6 | title = Antipain Y, a new antipain analog that inhibits neurotransmitter release from rat dorsal root ganglion neurons | journal = The Journal of Antibiotics | volume = 63 | issue = 1 | pages = 41–44 | date = January 2010 | pmid = 19911027 | doi = 10.1038/ja.2009.109 | doi-access = free }}</ref>

== References ==

{{reflist}}

[[Category:Peptides]]

[[Category:Aldehydes]]