Solid-state NMR spectroscopic analysis of the Ca 2+-dependent mannose binding of pradimicinA

Yu Nakagawa, Yuichi Masuda, Keita Yamada, Takashi Doi, K. Takegoshi, Yasuhiro Igarashi, Yukishige Ito

Research output: Contribution to journalArticlepeer-review

24 Citations (Scopus)


Aggregation facilitates analysis: The Ca 2+-dependent mannose (Man) binding of the nonpeptidic carbohydrate binder pradimicinA (PRM-A) was investigated in the solid state. The use of PRM-A aggregates eliminated problems associated with the three-component equilibrium. A combination of 113CdNMR spectroscopy and 2D dipolar-assisted rotational resonance revealed the mannose-binding site of PRM-A and the crucial role of the Ca 2+ ion (see binding model).

Original languageEnglish
Pages (from-to)6084-6088
Number of pages5
JournalAngewandte Chemie - International Edition
Issue number27
Publication statusPublished - 2011 Jun 27


  • antibiotics
  • carbohydrates
  • natural products
  • receptors
  • solid-state NMR spectroscopy

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

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