The effect of structural differences in the reducing terminus of sugars on the binding affinity of carbohydrates and proteins analyzed using photoaffinity labeling

Isao Ohtsuka, Yutaka Sadakane, Mari Higuchi, Noriyasu Hada, Junko Hada, Nobuko Kakiuchi, Akiyo Sakushima

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)

Abstract

Because carbohydrates and proteins bind with such low affinity, the nature of their interactions is not clear. Photoaffinity labeling with diazirin groups is useful for elucidating the roles of carbohydrates in these binding processes. However, when carbohydrate probes are synthesized according to this conventional method, the reducing terminus of the sugar is opened to provide an acyclic structure. Because greater elucidation of carbohydrate-protein interactions requires a closed-ring carbohydrate in addition to the photoreactive group, we synthesized new molecular tools. The carbohydrate ligands were synthesized in three steps (glycosylation with allyl alcohol, deprotection, and ozonolysis). Specific binding proteins for carbohydrate ligands were obtained by photoaffinity labeling. Closed ring-type carbohydrate ligands, in which the reducing sugar is closed, bound to lectins more strongly than open ring-type sugars. Carbohydrate to protein binding was observed using AFM.

Original languageEnglish
Pages (from-to)894-899
Number of pages6
JournalBioorganic and Medicinal Chemistry
Volume19
Issue number2
DOIs
Publication statusPublished - 2011 Jan 15

Keywords

  • Atomic force microscopy (AFM)
  • Carbohydrate-protein interaction
  • Molecular tools
  • Photoaffinity labeling

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmaceutical Science
  • Drug Discovery
  • Clinical Biochemistry
  • Organic Chemistry

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