Synthetic polymer analogues of enzymes characterized by esterase activity

Abstract

IT ~AS been reported [1, 2] that poly-4-vinylpyridines (poly-4-VP), partially alkylated with 2-(2'-ehloroethyl)pyridine or benzyl chloride, exert high catalytic activity in hydrolysis of the ester bond, which is 2.5-3.5 times greater than the catalytic activity of low molecular weight analogues. We explained this by the formation in macromolecular spheres of local cavities of polymer catalysts (PC), each of which incorporates a nueleophile (unalkylated pyridine ring) and is surrounded by hydrophobie groups, which have an increased affinity for the substrate. This paper describes results of detailed investigation of the relations of the action of similar PC containing different substituents: methyl, ethyl, propyl, isopropyl, butyl, isobutyl and isoamyl. As is well known, some of these substituents are contained in a-aminoacids (valine, alanine, leucine) and are often situated in direct proximity to active enzyme groups.