PubMed:10385973 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PubMed/sourceid/10385973","sourcedb":"PubMed","sourceid":"10385973","source_url":"http://www.ncbi.nlm.nih.gov/pubmed/10385973","text":"Conformational analysis of an alpha-galactosyl trisaccharide epitope involved in hyperacute rejection upon xenotransplantation.\nalpha-Galactosyl epitopes are carbohydrate structures bearing an alpha-Gal-(1--\u003e3)-Gal terminus (alpha-Gal epitopes). The interaction of these epitopes on the surface of animal cells with anti alpha-Gal antibodies in human serum is believed to be the main cause in antibody-mediated hyperacute rejection in xenotransplantation. In this paper, conformational analysis of an N-linked alpha-D-Galp-(1--\u003e3)-beta-D-Galp-(1--\u003e4)-beta-D-Glcp trisaccharide epitope was conducted in terms of each monosaccharide residue conformation, primary hydroxymethyl group configuration, and interglycosidic conformations. Selective 2D J-delta INEPT experiments have been carried out at three different temperatures to evaluate three-bond, long-range 13C-1H coupling constants for the crucial alpha-(1--\u003e3) linkage. The NMR experimental data were complemented by theoretical calculations. The flexibility and dynamics of the trisaccharide have been studied by Metropolis Monte Carlo simulations. Ensemble-averaged three-bond, long-range 13C-1H coupling constants and nuclear Overhauser effects were in good agreement with the experimental data. The alpha-(1--\u003e3) glycosidic linkage has shown a restricted flexibility as indicated by NMR spectroscopy and molecular 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