71136-37-3Relevant academic research and scientific papers
Protease inhibitors: Synthesis of matrix metalloproteinase and bacterial collagenase inhibitors incorporating 5-amino-2-mercapto-1,3,4-thiadiazole zinc binding functions
Scozzafava, Andrea,Supuran, Claudiu T
, p. 2667 - 2672 (2002)
Matrix metalloproteinase (MMP)/bacterial collagenase inhibitors incorporating 5-amino-2-mercapto-1,3,4-thiadiazole zinc binding functions are reported. A series of compounds was prepared by reaction of arylsulfonyl isocyanates or arylsulfonyl halides with phenylalanyl-alanine, followed by coupling with 5-amino-2-mercapto-1,3,4-thiadiazole in the presence of carbodiimides. These new compounds were assayed as inhibitors of human MMP-1, MMP-2, MMP-8 and MMP-9, and of the collagenase isolated from the anaerobe Clostridium histolyticum (ChC). The new derivatives proved to be powerful inhibitors of these metalloproteases, with activities in the low micromolar range for some of the target enzymes, depending on the substitution pattern at the arylsulfonyl(ureido) moieties.
A NEW FLUOROGENIC SUBSTRATE OF CARBOXYPEPTIDASE H - o-COUMAROYLPHENYLALANYLALANYLARGININE
Pozdnev, V. F.,Varlamov, O. L.,Grigor'yants, O. O.,Gomazkov, O. A.
, p. 213 - 218 (2007/10/02)
A new fluorogenic substrate is proposed for determining the enzymatic activity of carboxypeptidase H - o-coumaryl-L-phenylalanyl-L-alanyl-L-arginine (Cum-Phe-Ala-Arg-OH).The enzymatic hydrolysis of the substrate forms Cum-Phe-Ala-OH, which is determined f
