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Names | |
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IUPAC name
N2-{[(1S)-1-carboxy-2-phenylethyl]carbamoyl}-N5-(diaminomethylidene)-L-ornithyl-N-{(2S)-5-[(diaminomethylidene)amino]-1-oxopentan-2-yl}-L-valinamide
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Identifiers | |
3D model (
JSmol)
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ChemSpider | |
PubChem
CID
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UNII | |
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Properties | |
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).
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Antipain is an oligopeptide that is isolated from actinomycetes and used in biochemical research as a protease inhibitor of trypsin and papain. [1] It was discovered in 1972 and was the first natural peptide found that contained an ureylene group. [2] Antipain can aid in prevention of coagulation in blood. It is an inhibitor of serine and cysteine proteases. [3]
It has been crystallized in complexes with carboxypeptidase, which is obtained from wheat, [4] and Leishmania major oligopeptidase B. [5] 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. [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, 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 of antipain, which was isolated from a species of Streptomyces, inhibits the release of neurotransmitters in rat dorsal root ganglion neurons. [7]
![]() | |
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 | |
3D model (
JSmol)
|
|
ChemSpider | |
PubChem
CID
|
|
UNII | |
| |
| |
Properties | |
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).
|
Antipain is an oligopeptide that is isolated from actinomycetes and used in biochemical research as a protease inhibitor of trypsin and papain. [1] It was discovered in 1972 and was the first natural peptide found that contained an ureylene group. [2] Antipain can aid in prevention of coagulation in blood. It is an inhibitor of serine and cysteine proteases. [3]
It has been crystallized in complexes with carboxypeptidase, which is obtained from wheat, [4] and Leishmania major oligopeptidase B. [5] 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. [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, 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 of antipain, which was isolated from a species of Streptomyces, inhibits the release of neurotransmitters in rat dorsal root ganglion neurons. [7]