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Revision as of 22:02, 25 January 2024 editMarbletan (talk | contribs)Extended confirmed users5,633 edits someone has confused an unrelated clinical study titled "ANtiPain" with the topic of this article← Previous edit Revision as of 22:06, 25 January 2024 edit undoMarbletan (talk | contribs)Extended confirmed users5,633 edits different chemical compoundNext edit →
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It has been crystallized in complexes with ], which is obtained from ],<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 '']'' ] 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 ] of antipain forms a covalent bond to the active site ] in the protease. It has been crystallized in complexes with ], which is obtained from ],<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 '']'' ] 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 ] of antipain forms a covalent bond to the active site ] in the protease.

⚫ A recent research article indicated that antipain Y is a new type of anti-pain analog, which can inhibit the release of neurotransmitter 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>


A study was performed for information on the effect of antipain on the quality of post-thawed ram ].<ref name=Akhtarshenas>{{Cite journal | doi = 10.1111/rda.13253 }}</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 ], permitting this substance to be able to improve the resistance of membrane disruption by freezing temperatures.<ref name=Akhtarshenas/> A study was performed for information on the effect of antipain on the quality of post-thawed ram ].<ref name=Akhtarshenas>{{Cite journal | doi = 10.1111/rda.13253 }}</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 ], 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 ] of antipain, which was isolated from a species of '']'', 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 == == References ==

Revision as of 22:06, 25 January 2024

This article is about the protease inhbitor. For the article about pain relief, see analgesic.
Antipain
Names
IUPAC name N-{carbamoyl}-N-(diaminomethylidene)-L-ornithyl-N-{(2S)-5--1-oxopentan-2-yl}-L-valinamide
Identifiers
CAS Number
3D model (JSmol)
ChemSpider
PubChem CID
UNII
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/s1Key: SDNYTAYICBFYFH-TUFLPTIASA-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/s1Key: SDNYTAYICBFYFH-TUFLPTIABE
SMILES
  • O=C(NC(=O)(NC(=O)(NC(=O)N(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
Except where otherwise noted, data are given for materials in their standard state (at 25 °C , 100 kPa). ☒N verify (what is  ?) Infobox references
Chemical compound

Antipain is an oligopeptide that is isolated from actinomycetes and used in biochemical research as a protease inhibitor of trypsin and papain. It was discovered in 1972 and was the first natural peptide found that contained an ureylene group. Antipain can aid in prevention of coagulation in blood. It is an inhibitor of serine and cysteine proteases.

It has been crystallized in complexes with carboxypeptidase, which is obtained from wheat, and Leishmania major oligopeptidase B. 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. The results from this experiment concluded that antipain aided in the quality of ram semen by maintaining the sperm mobility. 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.

Antipain Y, a similar chemical compound that is an analog of antipain, which was isolated from a species of Streptomyces, inhibits the release of neurotransmitters in rat dorsal root ganglion neurons.

References

  1. Suda H, Aoyagi T, Hamada M, Takeuchi T, Umezawa H (April 1972). "Antipain, a new protease inhibitor isolated from actinomycetes". The Journal of Antibiotics. 25 (4): 263–266. doi:10.7164/antibiotics.25.263. PMID 4559651.
  2. Umezawa S, Tatsuta K, Fujimoto K, Tsuchiya T, Umezawa H (April 1972). "Structure of antipain, a new Sakaguchi-positive product of streptomyces". The Journal of Antibiotics. 25 (4): 267–270. doi:10.7164/antibiotics.25.267. PMID 5052959.
  3. Lackie J (2012). A Dictionary of Biomedicine. Oxford University Press. ISBN 9780199549351.
  4. PDB ENTRY 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:10.1006/jmbi.1996.0058. PMID 8636973.
  5. PDB ENTRY 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". The Journal of Biological Chemistry. 285 (50): 39249–39259. doi:10.1074/jbc.M110.156679. PMC 2998157. PMID 20926390.
  6. ^ . doi:10.1111/rda.13253. {{cite journal}}: Cite journal requires |journal= (help); Missing or empty |title= (help)
  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". The Journal of Antibiotics. 63 (1): 41–44. doi:10.1038/ja.2009.109. PMID 19911027.
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