Description
Bestatin HCl (65391-42-6) inhibits leucine aminopeptidase and aminopeptidases B and N. Inhibits leukotriene A4 hydrolase. Displays immunostimulant activity via activation of macrophages and T lymphocytes. Displays antitumor activity.
Uses
Bestatin has been used as a protease inhibitor for the purification of his-tagged Tau protein.
Uses
Bestatin is an inhibitor of amino peptidases and a potent, irreversible inhibitor of LTA4 hydrolase. It inhibits the amino peptidase activity of LTA4 hydrolase with a Ki value of 201 nM. It offers promise as a novel analgesic because it protects endogenous opioid peptides against degradation. It does not inhibit carboxypeptidases.
Uses
competitive aminopeptidase B inhibitor
Definition
ChEBI: Bestatin (hydrochloride) is a peptide.
General Description
Chemical structure: amino acid derivatives
Biochem/physiol Actions
A metalloprotease inhibitor selective for aminopeptidase. Bestatin is a competitive and specific inhibitor of leucine aminopeptidase, aminopeptidase B, and triamino peptidase. It inhibits aminopeptidase B at 60 nM (using arginine-β-naphthylamide as substrate) and leucine aminopeptidase at 20 nM (leucine-β-naphthylamide as substrate). It showed no inhibition of aminopeptidase A, trypsin, chymotrypsin, elastase, papain, pepsin, or themolysin. It offers promise as a novel analgesic because it protects endogenous opioid peptides against degradation.
in vivo
in a mouse dorsal air sac assay, oral administration of bestatin (100-200 mg/kg/day) showed a significant inhibitory activity against the melanoma cell-induced angiogenesis. bestatin also inhibited the tube-like formation of human umbilical vein endothelial cells (huvecs). furthermore, after the orthotopic implantation of b16-bl6 melanoma cells into mice, bestatin administration (50-100 mg/kg/day, i.p) reduced the number of vessels oriented towards the established primary tumor mass on the dorsal side of mice [1].
References
1) Orning et al. (1991), Leukotriene A4 hydrolase. Inhibition by bestatin and intrinsic aminopeptidase activity establish its functional resemblance to metallohydrolase enzymes; J. Biol. Chem., 266 1375
2) Wang et al. (2010), The effect of different species aminopeptidase N structure on the activity screening of aminopeptidase N inhibitor; Biol. Pharm. Bull., 33 1658
