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Three 2-acetamido-2-deoxy-α-d-galactopyranoses attached to Ser2, Thr3 Thr4 of the amino-terminal portion of glycophorin AM are responsible for the so-called TN blood group specificity. The corresponding glycopeptide H2N-Ser-Se*r-Th*r-Th*r-Gly-OH obtained by a stepwise peptide coupling strategy was submitted to a detailed high-field nuclear magnetic resonance (n.m.r.) analysis. 13C-n.m.r. spectrum confirms the validity of previous assignments made on M sialo and asialoglycopeptides obtained by specific degradation of human glycophorin AM. In addition, the 400 MHz 1H-n.m.r. spectrum allowed most of the proton resonances to be assigned. A careful examination of the chemical shifts and coupling constants revealed some interesting features of the conformational properties of the GalNAc-Ser and GalNAc-Thr linkage as well as of the rotational isomerism of Thr and Ser side-chains. The data give conclusive evidence that high-field n.m.r. spectroscopy can be successfully used to gain structural and dynamic information on rather sophisticated glycopeptides.
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Pavia et al. (2009) studied this question.
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