chymostatin

Chymostatin is a naturally occurring peptide aldehyde protease inhibitor produced by certain Streptomyces species. It is a mixture of hydrophobic tetrapeptide aldehydes with three principal components (A, B, and C), differing by one amino acid residue. Chymostatin potently inhibits several serine and cysteine proteases including chymotrypsin, chymotrypsin-like serine proteinases, cathepsins B/H/L/G (notably cathepsin G), papain, and chymases. It acts as a competitive inhibitor at the active site of these enzymes. Chymostatin has been used primarily in research to study protease function and inhibition; it exhibits anti-inflammatory effects by reducing pro-inflammatory cytokines such as IL‐1β and IL‐6 and shows protective effects in models of acute lung injury as well as anticancer activity against lung cancer cells[1][4][10]. It is not approved for clinical use in humans.

Other names

N-(Nα-Carbonyl-Cpd-X-Phe-al)-Phe(2S)-2-[[(1S)-1-(2-amino-1,4,5,6-tetrahydropyrimidin-6-yl)-2-[[(1S)-1-[[(1S)-1-benzyl-2-oxo-ethyl]carbamoyl]-3-methyl-butyl]amino]-2-oxo-ethyl]carbamoylamino]-3-phenyl-propanoic acid(2S)-2-{[(S)-(2-imino-1,3-diazinan‑4‑yl)({[(1S)‑3‑methyl‑1-{[(2S)‑1‑oxo‑3‑phenylpropan‑2–yl]carbamoyl}butyl]carbamoyl})methyl]carbamoyl}amino}-3–phenylpropanoic acidW7MU4REM7L (UNII)