Open AccessHigh-Affinity Glycopolymer Binding to Human DC-SIGN and Disruption of DC-SIGN Interactions with HIV Envelope Glycoprotein
Author(s) -
C. Remzi Becer,
Matthew I. Gibson,
Jin Geng,
Rebecca Ilyas,
Russell Wallis,
Daniel A. Mitchell,
David M. Haddleton
Publication year - 2010
Publication title -
journal of the american chemical society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.115
H-Index - 612
eISSN - 1520-5126
pISSN - 0002-7863
DOI - 10.1021/ja1056714
Subject(s) - dc sign , glycopolymer , chemistry , glycoprotein , lectin , biophysics , click chemistry , glycosylation , sign (mathematics) , viral envelope , envelope (radar) , polymerization , biochemistry , combinatorial chemistry , dendritic cell , immune system , polymer , immunology , organic chemistry , mathematical analysis , telecommunications , radar , mathematics , computer science , biology
Noncovalent interactions between complex carbohydrates and proteins drive many fundamental processes within biological systems, including human immunity. In this report we aimed to investigate the potential of mannose-containing glycopolymers to interact with human DC-SIGN and the ability of these glycopolymers to inhibit the interactions between DC-SIGN and the HIV envelope glycoprotein gp120. We used a library of glycopolymers that are prepared via combination of copper-mediated living radical polymerization and azide-alkyne [3+2] Huisgen cycloaddition reaction. We demonstrate that a relatively simple glycopolymer can effectively prevent the interactions between a human dendritic cell associated lectin (DC-SIGN) and the viral envelope glycoprotein gp120. This approach may give rise to novel insights into the mechanisms of HIV infection and provide potential new therapeutics.
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