PEGylation near a Patch of Nonpolar Surface Residues Increases the Conformational Stability of the WW Domain
Year: 2019
Type: article
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.
Source: The Journal of Organic Chemistry
Authors: Steven R. E. Draper, Dallin S. Ashton, Benjamin M. Conover, Anthony J. Carter, Kimberlee L. Stern, Qiang Xiao, Joshua L. Price
Institution: Brigham Young University
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: green
OpenAlex ID: W2990936628