Antipain


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.
It has been crystallised 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.

Antiretroviral and Protease inhibitors

There are several Serine proteases, which are enzymes that cleave the protein bond, in the human genome. The abnormal functioning of these proteases can lead to the development of cancerous tumors . Protease inhibitors or antipain are enzymes that are used to regulate their performance.
The antiretroviral drug Nelfinavir is one example of an antipain. It was classified as an antipain after a study published by Ovid that investigated the in vitro effect of Nelfinavir using and found that it selectively inhibited HER2- positive, a growth factor in breast cancer.

Protease inhibitors and DRUG neurons

Protease-activated receptors are a unique class of G protein-coupled receptors activated by proteolytic cleavage of the receptor N terminus. PARs are activated by some Serine Proteases and are important for the physiological, , and pathological functions of the human body.
During the study, an antipain analogue Y was developed and studied. It was shown to have properties as a protease inhibitors but it had a low IC50 than a antipain. Antipain analogue Y was able to suppress Trypsin, which inhibits the secretion of an excitatory neuropeptide that leads to inflammation and other disorders.