Publikation: Molecular analysis of Carbohydrate−Antibody interactions : case study using a Bacillus anthracis Tetrasaccharide
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2010
Autor:innen
Oberli, Matthias A.
Tamborrini, Marco
Tsai, Yu-Hsuan
Werz, Daniel B.
Horlacher, Tim
Adibekian, Alexander
Pluschke, Gerd
Seeberger, Peter H.
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Journal of the American Chemical Society. 2010, 132(30), pp. 10239-10241. ISSN 0002-7863. eISSN 1520-5126. Available under: doi: 10.1021/ja104027w
Zusammenfassung
The process for selecting potent and effective carbohydrate antigens is not well-established. A combination of synthetic glycan microarray screening, surface plasmon resonance analysis, and saturation transfer difference NMR spectroscopy was used to dissect the antibody-binding surface of a carbohydrate antigen, revealing crucial binding elements with atomic-level detail. This analysis takes the first step toward uncovering the rules for structure-based design of carbohydrate antigens.
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OBERLI, Matthias A., Marco TAMBORRINI, Yu-Hsuan TSAI, Daniel B. WERZ, Tim HORLACHER, Alexander ADIBEKIAN, Dominik GAUSS, Heiko M. MÖLLER, Gerd PLUSCHKE, Peter H. SEEBERGER, 2010. Molecular analysis of Carbohydrate−Antibody interactions : case study using a Bacillus anthracis Tetrasaccharide. In: Journal of the American Chemical Society. 2010, 132(30), pp. 10239-10241. ISSN 0002-7863. eISSN 1520-5126. Available under: doi: 10.1021/ja104027wBibTex
@article{Oberli2010-08-04Molec-12611,
year={2010},
doi={10.1021/ja104027w},
title={Molecular analysis of Carbohydrate−Antibody interactions : case study using a Bacillus anthracis Tetrasaccharide},
number={30},
volume={132},
issn={0002-7863},
journal={Journal of the American Chemical Society},
pages={10239--10241},
author={Oberli, Matthias A. and Tamborrini, Marco and Tsai, Yu-Hsuan and Werz, Daniel B. and Horlacher, Tim and Adibekian, Alexander and Gauss, Dominik and Möller, Heiko M. and Pluschke, Gerd and Seeberger, Peter H.}
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<dc:contributor>Pluschke, Gerd</dc:contributor>
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<dcterms:abstract xml:lang="eng">The process for selecting potent and effective carbohydrate antigens is not well-established. A combination of synthetic glycan microarray screening, surface plasmon resonance analysis, and saturation transfer difference NMR spectroscopy was used to dissect the antibody-binding surface of a carbohydrate antigen, revealing crucial binding elements with atomic-level detail. This analysis takes the first step toward uncovering the rules for structure-based design of carbohydrate antigens.</dcterms:abstract>
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