202344-80-7

Upstream product

• 113543-30-9 (S)-4-benzyl-3-(4-methylpentanoyl)oxazolidin-2-one 
• 106-95-6 allyl bromide 

Relevant academic research and scientific papers

Development of novel G-protein-coupled receptor 54 agonists with resistance to degradation by matrix metalloproteinase

Kisspeptin-GPR54 signaling is involved in the suppression of cancer metastasis and regulation of hormonal secretion. Recently, matrix metalloproteinase mediated deactivation of kisspeptins through hydrolysis of the Gly-Leu peptide bond has been reported.

MERCAPTOKETONES AND MERCAPTOALCOHOLS AND A PROCESS FOR THEIR PREPARATION

This invention relates to matrix metalloproteinase (MMP) inhibiting compounds of the formula: STR1 where R 1 is C 1-C 12 alkyl, straight or branched and optionally substituted by halogen, hydroxy, C. sub.1-C 6 alkoxy, amino, carboxyl, C 1-C. sub.6 alkoxycarbonyl, carboxamido, nitrile, mono-or di-(C 1-C 6) alkylamino, thio, C 1-C 6 alkylthio, aryl,--Oaryl or--OCH. sub. 2 aryl where aryl is optionally substituted with C 1-C 6 alkyl, C 1-C 6 alkoxy, carboxy, halogen, cyano, nitro, carboxamido, or hydroxy; and C 1-C. sub.6 alkanesulfonyloxy. R 2 is α-OH or β-OH and R 6 is H or R. sup.2 and R 6 together are carbonyl; the chemical intermediates; and processes for the preparation of these compounds and the intermediates thereto. Matrix metalloproteinases (MMP) are a family of zinc-containing calcium dependent proteinases, including stromelysins, collagenases, and gelatinases. These MMP enzymes are capable of degrading the proteinaceous components of connective tissue and appear to be involved in tissue remodeling, i.e., wound healing and connective tissue turnover. Unexpectedly, the mercaptoalcohols with the S-configuration at the hydroxyl-bearing carbon have been found to be at least 4 times more potent than the analogous (R)-alcohols both in vitro and in vivo in inhibiting the MMP enzyme.

Mercaptoketones and mercaptoalcohols, a process for their preparation and their use as inhibitors of matrix metalloproteinases

This invention relates to matrix metalloproteinase (MMP) inhibiting compounds of the formula: where R1is C1-C12alkyl, straight or branched and optionally substituted by halogen, hydroxy, C1-C6alkoxy, amino, carboxyl, C1-C6alkoxycarbonyl, carboxamido, nitrile, mono- or di-(C1-C6)alkylamino, thio, C1-C6alkylthio, aryl, -Oaryl or -OCH2aryl where aryl is optionally substituted with C1-C6alkyl, C1-C6alkoxy, carboxy, halogen, cyano, nitro, carboxamido, or hydroxy; and C1-C6alkanesulfonyloxy. R2is α-OH or β-OH and R6is H or R2and R6together are carbonyl; the chemical intermediates; and processes for the preparation of these compounds and the intermediates thereto. Matrix metalloproteinases (MMP) are a family of zinc-containing calcium dependent proteinases, including stromelysins, collagenases, and gelatinases. These MMP enzymes are capable of degrading the proteinaceous components of connective tissue and appear to be involved in tissue remodeling, i.e., wound healing and connective tissue turnover. Unexpectedly, the mercaptoalcohols with the S-configuration at the hydroxyl-bearing carbon have been found to be at least 4 times more potent than the analogous (R)-alcohols both in vitroand in vivoin inhibiting the MMP enzyme..

The asymmetric synthesis and in vitro characterization of succinyl mercaptoalcohol and mercaptoketone inhibitors of matrix metalloproteinases

A series of succinyl based mercaptoketones and diastereomeric mercaptoalcohols were prepared and evaluated in vitro as inhibitors of the matrix metalloproteinases collagenase-1 (MMP-1), stromelysin (MMP-3), and gelatinase-B (MMP-9).