Issue 12, 2005
From the journal:

Organic & Biomolecular Chemistry

Cyanovirin-N binding to Manα1–2Man functionalized dendrimers†

Shane L. Mangold,a   Joel R. Morgan,a   Gregory C. Strohmeyer,a   Angela M. Gronenbornb  and  Mary J. Cloninger*a  

* Corresponding authors

a Department of Chemistry and Biochemistry and Center for Bioinspired Nanomaterials, 108 Gaines Hall, Montana State University, Bozeman, MT, USA
E-mail: mcloninger@chemistry.montana.edu
Fax: 406 994 5407
Tel: 406 994 3051

b Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD

Abstract

Manα1–2Man functionalized G(3) and G(4)–PAMAM dendrimers have been synthesized and characterized by MALDI-TOF MS and NMR spectroscopy. Precipitation assays to assess the binding of the dimannose-functionalized dendrimers to Cyanovirin-N, a HIV-inactivating protein that blocks virus-to-cell fusion through high mannose mediated interactions, are presented.

Graphical abstract: Cyanovirin-N binding to Manα1–2Man functionalized dendrimers

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Article information

DOI
https://doi.org/10.1039/B417789D
Article type
Paper
Submitted
30 Nov 2004
Accepted
04 May 2005
First published
24 May 2005

Org. Biomol. Chem., 2005,3, 2354-2358

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Cyanovirin-N binding to Manα1–2Man functionalized dendrimers

S. L. Mangold, J. R. Morgan, G. C. Strohmeyer, A. M. Gronenborn and M. J. Cloninger, Org. Biomol. Chem., 2005, 3, 2354 DOI: 10.1039/B417789D

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