Carbohydrate recognition of gramicidin S analogues in aqueous medium

We have designed and synthesized of carbohydrate-binding peptides. gramicid in S analogues. Asn/Asp/Gln and Trp residues in the peptides were employed as the binding sites for carbohydrates by hydrogen-bonding interaction and the creation units for hydrophobic pocket to promote the interaction, respe ctively. The data of fluorescence spectroscopy and affinity column chromato graphy indicated that the peptides possessed the binding ability for some c arbohydrates in aqueous medium. As a result of H-1 NMR study, nuclear Overh auser effects between aromatic side chains of a peptide. [Gln(1.1 '),Trp(3. 3 ')]-gramisidin S and mannose were observed. indicating that the interacti on of the peptide with the sugar occurred in the hydrophobic environment fo rmed by Trp and Phe residues. (C) 2001 Elsevier Science Ltd. All rights res erved.