ENGINEERING OF CYCLIC-PEPTIDES WITH NOVEL INHIBITING PROPERTIES TO DIFFERENTIATE 2 SERINE PROTEASES, CHYMOTRYPSIN-CARLSBERG AND SUBTILISIN-CARLSBERG

[摘要] Based on the crystal structure of the inhibitory loop of barley chymotrypsin inhibitor II (Cl-II), two cyclic peptides, (I) under bar-1 and (I) under bar-2, were designed and synthesized chemically. (I) under bar-1 is a noncompetitive inhibitor for chymotrypsin and uncompetitive inhibitor for subtilisin Carlsberg. (I) under bar-2 exhibited competitive inhibition of both chymotrypsin end subtilisin Carlsberg. The results indicate that the hydrophobic region of the inhibitory loop of Cl-II plays an important role for Cl-II to bind to the active sites of proteases.

[发布日期] 1994-09-08