PEGylation near a Patch of Nonpolar Surface Residues Increases the Conformational Stability of the WW Domain.

ABSTRACT: Many proteins have one or more surface-exposed patches of nonpolar residues; our observations here suggest that PEGylation near such locations might be a useful strategy for increasing protein conformational stability. Specifically, we show that conjugating a PEG-azide to a propargyloxyphenylalanine via the copper(I)-catalyzed azide-alkyne cycloaddition can increase the conformational stability of the WW domain due to a favorable synergistic effect that depends on the hydrophobicity of a nearby patch of nonpolar surface residues.

SUBMITTER: Draper SRE 

PROVIDER: S-EPMC8147659 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature