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

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journal contribution
posted on 09.12.2019, 05:29 by Steven R. E. Draper, Dallin S. Ashton, Benjamin M. Conover, Anthony J. Carter, Kimberlee L. Stern, Qiang Xiao, Joshua L. Price
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.

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