Association of (+)-catechin and catechin-(4α → 8)-catechin with oligopeptides

Tsutomu Hatano; Richard W. Hemingway

doi:10.1039/CC9960002537

Association of (+)-catechin and catechin-(4α → 8)-catechin with oligopeptides

Tsutomu Hatano, Richard W. Hemingway

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

33 Citations (Scopus)

Abstract

NOE studies on the complexation of (poly)flavanoids with peptides containing proline residues in aqueous solutions reveal site specific approach directed by hydrophobic interaction of the aromatic rings of catechin and its dimer, catechin-(4α → 8)-catechin, to conformationally accessible regions of peptides without strong preference for interaction with proline residues.

Original language	English
Pages (from-to)	2537-2538
Number of pages	2
Journal	Chemical Communications
Issue number	22
DOIs	https://doi.org/10.1039/CC9960002537
Publication status	Published - Jan 1 1996

ASJC Scopus subject areas

Catalysis
Electronic, Optical and Magnetic Materials
Ceramics and Composites
Chemistry(all)
Surfaces, Coatings and Films
Metals and Alloys
Materials Chemistry

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10.1039/CC9960002537

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title = "Association of (+)-catechin and catechin-(4α → 8)-catechin with oligopeptides",

abstract = "NOE studies on the complexation of (poly)flavanoids with peptides containing proline residues in aqueous solutions reveal site specific approach directed by hydrophobic interaction of the aromatic rings of catechin and its dimer, catechin-(4α → 8)-catechin, to conformationally accessible regions of peptides without strong preference for interaction with proline residues.",

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AU - Hemingway, Richard W.

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N2 - NOE studies on the complexation of (poly)flavanoids with peptides containing proline residues in aqueous solutions reveal site specific approach directed by hydrophobic interaction of the aromatic rings of catechin and its dimer, catechin-(4α → 8)-catechin, to conformationally accessible regions of peptides without strong preference for interaction with proline residues.

AB - NOE studies on the complexation of (poly)flavanoids with peptides containing proline residues in aqueous solutions reveal site specific approach directed by hydrophobic interaction of the aromatic rings of catechin and its dimer, catechin-(4α → 8)-catechin, to conformationally accessible regions of peptides without strong preference for interaction with proline residues.

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Association of (+)-catechin and catechin-(4α → 8)-catechin with oligopeptides

Abstract

ASJC Scopus subject areas

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