Structural, dynamic, and metal-ion binding studies of the core glycopeptides beta-D-Gal-(1----3)-alpha-D-GalNAc----Ser, Thr by 13C-N.m.r. spectroscopy |
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| Authors: | K Dill H K Lannom M Denarié J M Lacombe A A Pavia |
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| Affiliation: | Department of Chemistry, Clemson University, Clemson, S.C. 29631 U.S.A.;Laboratoire de Chimie Bioorganique, Faculté des Sciences, 33, rue Louis Pasteur, 84000 Avignon France |
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| Abstract: | 13C-N.m.r. spectral data as well as spin-lattice relaxation times (T1 values) are presented for the core glycopeptides beta-D-Gal-(1----3)-alpha-D-GalNAc----Ser, Thr. The binding of Gd3+ to these model compounds containing N-terminal blocking groups and esterified carboxyl groups indicates that the disaccharide contains a rather weak, but unique, binding-site in the vicinity of C-2 of alpha-D-GalNAc (possibly involving N-2', the acetamido carbonyl group, O-3' and/or possibly the glycosidic oxygen atom (O-3)). |
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| Keywords: | To whom correspondence should be addressed |
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