A Versatile and Robust Serine Protease Inhibitor Scaffold from Actinia tenebrosa.

ABSTRACT: Serine proteases play pivotal roles in normal physiology and a spectrum of patho-physiological processes. Accordingly, there is considerable interest in the discovery and design of potent serine protease inhibitors for therapeutic applications. This led to concerted efforts to discover versatile and robust molecular scaffolds for inhibitor design. This investigation is a bioprospecting study that aims to isolate and identify protease inhibitors from the cnidarian Actinia tenebrosa. The study isolated two Kunitz-type protease inhibitors with very similar sequences but quite divergent inhibitory potencies when assayed against bovine trypsin, chymostrypsin, and a selection of human sequence-related peptidases. Homology modeling and molecular dynamics simulations of these inhibitors in

SUBMITTER: Chen X 

PROVIDER: S-EPMC6950308 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature