Saturation-transfer difference NMR studies for the epitope mapping of a carbohydrate-mimetic peptide recognized by an anti-carbohydrate antibody.
作者信息
Johnson Margaret A, Pinto B Mario
机构信息
Departments of Chemistry and of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, BC, Canada V5A 1S6.
出版信息
Bioorg Med Chem. 2004 Jan 2;12(1):295-300. doi: 10.1016/j.bmc.2003.09.041.
PMID:14697795
Abstract
Saturation-transfer difference NMR spectroscopy (STD-NMR) experiments have been performed to analyze the topography or epitope of the octapeptide MDWNMHAA recognized by the anti-carbohydrate antibody SYA/J6 in solution; the antibody is directed against the Shigella flexneri Y O-antigen polysaccharide. The results permit a valuable comparison of solution versus crystal-structure data, and provide insight for the design of the next-generation binding ligands.
摘要
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