High-affinity glycopolymer binding to human DC-SIGN and disruption of DC-SIGN interactions with HIV envelope glycoprotein
Becer, C. Remzi, Gibson, Matthew I., Geng, Jin, Ilyas, Rebecca, Wallis, Russell, Mitchell, Daniel Anthony and Haddleton, David M.. (2010) High-affinity glycopolymer binding to human DC-SIGN and disruption of DC-SIGN interactions with HIV envelope glycoprotein. Journal of the American Chemical Society, Vol.132 (No.43). pp. 15130-15132. ISSN 0002-7863Full text not available from this repository.
Official URL: http://dx.doi.org/10.1021/ja1056714
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-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.
|Item Type:||Journal Article|
|Subjects:||Q Science > QD Chemistry|
|Divisions:||Faculty of Science > Chemistry|
|Library of Congress Subject Headings (LCSH):||Polymerization, Glycoproteins, Glycomics, Viral envelopes|
|Journal or Publication Title:||Journal of the American Chemical Society|
|Publisher:||American Chemical Society|
|Official Date:||3 November 2010|
|Number of Pages:||3|
|Page Range:||pp. 15130-15132|
|Funder:||European Union (EU), University of Warwick, Wellcome Trust (London, England)|
|Grant number:||235999 (EU), 077400 (WT)|
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