Synthesis and structure-activity study of protease inhibitors. III. Amidinophenols and their benzoil esters.
- 1 January 1984
- journal article
- research article
- Published by Pharmaceutical Society of Japan in CHEMICAL & PHARMACEUTICAL BULLETIN
- Vol. 32 (11) , 4466-4477
- https://doi.org/10.1248/cpb.32.4466
Abstract
Various amidinophenol derivatives and their benzoates were synthesized and evaluated for inhibitory activities against trypsin, plasmin, kallikrein, thrombin, Cl.hivin.r and Cl.hivin.s [activated complement components C1s and C1r] as well as in vitro complement-mediated hemolysis. 4-(.beta.-Amidinoethenyl)phenyl 4-guanidinobenzoate and 4-amidino-2-benzoylphenyl 4-guanidinobenzoate had potent inhibitory activities with IC50 [median inhibitory concentration] of 9 .times. 10-8 M (trypsin) and 2 .times. 10-7 M (Cl.hivin.s) for the former and 3 .times. 10-8 M (trypsin) and 2 .times. 10-7 M (Cl.hivin.s) for the latter.This publication has 5 references indexed in Scilit:
- Synthesis and structure-activity study of protease inhibitors. I. (Guanidinophenyl)propionate and guanidinocinnamate derivatives.CHEMICAL & PHARMACEUTICAL BULLETIN, 1984
- Inhibition of four human serine proteases by substituted benzamidinesJournal of Medicinal Chemistry, 1978
- Synthetic inhibitors of trypsin, plasmin, kallikrein, thrombin, , and C1 esteraseBiochimica et Biophysica Acta (BBA) - Enzymology, 1977
- Proteolytic enzymes. 7. "Inverse substrates" for trypsin. Efficient enzymic hydrolysis of certain esters with a cationic center in the leaving groupJournal of the American Chemical Society, 1977
- The Role of Cl Esterase Inhibitor in the Activation of Clr, a Subcomponent of the First Component of Complement from Human PlasmaThe Journal of Biochemistry, 1976