Protease-Catalyzed l-Aspartate Oligomerization: Substrate Selectivity and Computational Modeling.

ABSTRACT: Poly(aspartic acid) (PAA) is a biodegradable water-soluble anionic polymer that can potentially replace poly(acrylic acid) for industrial applications and has shown promise for regenerative medicine and drug delivery. This paper describes an efficient and sustainable route that uses protease catalysis to convert l-aspartate diethyl ester (Et₂-Asp) to oligo(β-ethyl-α-aspartate), oligo(β-Et-α-Asp). Comparative studies of protease activity for oligo(β-Et-α-Asp) synthesis revealed α-chymotrypsin to be the most efficient. Papain, which is highly active for l-glutamic acid diethyl ester (Et₂-Glu) oligomerization, is inactive for Et₂-Asp oligomerization. The assignment of α-linkages between aspartate repeat units formed by α-chymotrypsin catalysis is based on nucl

SUBMITTER: Yang F 

PROVIDER: S-EPMC7066554 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature