K. Fok, J. A. Yankeelov
Jan 10, 1977
Citations
0
Influential Citations
5
Citations
Journal
Biochemical and biophysical research communications
Abstract
Abstract A non-hydrolyzable analogue of the dipeptide glycylleucine has been prepared which contains a thiomethylene group substituted for the peptide linkage. The affinity of the analogue (( S )-2-(S-cysteaminyl)-4-methylpentoic acid) for aminopeptidase M is four-fold greater than that of Gly-Leu. Inhibition of the hydrolysis of glycine-p-nitroanilide is competitive. This analogue represents the first member of a new class of compounds which conserves both charge and conformation of the parent compound while presenting a non-hydrolyzable linkage at the normal point of cleavage in a peptide substrate. Analogues of this type may have potential for the design of inhibitors which utilize contiguous enzyme binding sites complementary to both sides of the point of cleavage in normal substrates of proteolytic enzymes.