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

Steven R. E. Draper | Zendy; Dallin S. Ashton | Zendy; Benjamin M. Conover | Zendy; Anthony J. Carter | Zendy; K.L. Stern | Zendy; Qiang Xiao | Zendy; Joshua L. Price | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

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

Author(s) -

Steven R. E. Draper,

Dallin S. Ashton,

Benjamin M. Conover,

Anthony J. Carter,

K.L. Stern,

Qiang Xiao,

Joshua L. Price

Publication year - 2019

Publication title -

the journal of organic chemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.2

H-Index - 228

eISSN - 1520-6904

pISSN - 0022-3263

DOI - 10.1021/acs.joc.9b02615

Subject(s) - chemistry , pegylation , azide , cycloaddition , stereochemistry , biophysics , catalysis , organic chemistry , polyethylene glycol , biology

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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research