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

doi:10.1002/anie.201007775

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

PHA - Molecular Pharmaceutical Science

Research output: Contribution to journal › Article › peer-review

27 Citations (Scopus)

Abstract

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 language	English
Pages (from-to)	6084-6088
Number of pages	5
Journal	Angewandte Chemie - International Edition
Volume	50
Issue number	27
DOIs	https://doi.org/10.1002/anie.201007775
Publication status	Published - 2011 Jun 27

Keywords

antibiotics
carbohydrates
natural products
receptors
solid-state NMR spectroscopy

ASJC Scopus subject areas

Catalysis
Chemistry(all)

Access to Document

10.1002/anie.201007775

Cite this

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abstract = "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).",

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AU - Nakagawa, Yu

AU - Masuda, Yuichi

AU - Yamada, Keita

AU - Doi, Takashi

AU - Takegoshi, K.

AU - Igarashi, Yasuhiro

AU - Ito, Yukishige

PY - 2011/6/27

Y1 - 2011/6/27

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AB - 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).

KW - antibiotics

KW - carbohydrates

KW - natural products

KW - receptors

KW - solid-state NMR spectroscopy

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