Issue 6, 2011
From the journal:

Molecular BioSystems

Interaction of natural polyphenols with α-amylase in vitro: molecular property–affinity relationship aspect

Jianbo Xiao,*ab   Guoyin Kai,a   Xiaoling Ni,c   Fan Yanga  and  Xiaoqing Chen*d  

* Corresponding authors

a Department of Biology, College of Life & Environment Science, Shanghai Normal University, 100 Guilin Rd, Shanghai 200234, PR China
E-mail: jianboxiao@yahoo.com
Fax: +86 (021) 64321291
Tel: +86 (136) 11600163

b Department of Nutrition, Faculty of Health and Welfare, Okayama Prefectural University, Soja, Okayama, Japan

c Department of General Surgery, Zhongshan Hospital, Fudan University, Shanghai 200032, PR China

d College of Chemistry and Chemical Engineering, Central South University, Changsha 410083, PR China
E-mail: xqchen@mail.csu.edu.cn
Tel: +86 (731) 8830833

Abstract

The relationship between the structural properties of natural polyphenols and their affinities for α-amylase were investigated by fluorescence titration analysis. The binding process with α-amylase was strongly influenced by the structural differences of the compounds under study. For instance, the methylation of the hydroxyl group in flavonoids increased their binding affinities for α-amylase by 2.14 to 7.76 times. The hydroxylation on rings A, B, and C of flavonoids also significantly affected their affinities for α-amylase. The glycosylation of isoflavones and flavanones reduced their affinities for α-amylase and the glycosylation of flavones and flavonols enhanced their affinities for α-amylase. Hydrogenation of the C2[double bond, length as m-dash]C3 double bond of flavonoids decreased the binding affinities. The galloylated catechins had higher binding affinities with α-amylase than non-galloylated catechins and the pyrogallol-type catechins had higher affinities than the catechol-type catechins. The presence of the galloyl moiety is the most decisive factor. The glycosylation of resveratrol decreased its affinity for α-amylase. The esterification of gallic acid significantly reduced the affinity for α-amylase. The binding interaction between polyphenols and α-amylase was mainly caused by hydrophobic forces.

Graphical abstract: Interaction of natural polyphenols with α-amylase in vitro: molecular property–affinity relationship aspect

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Article information

DOI
https://doi.org/10.1039/C1MB05008G
Article type
Paper
Submitted
10 Jan 2011
Accepted
18 Feb 2011
First published
29 Mar 2011

Mol. BioSyst., 2011,7, 1883-1890

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Interaction of natural polyphenols with α-amylase in vitro: molecular property–affinity relationship aspect

J. Xiao, G. Kai, X. Ni, F. Yang and X. Chen, Mol. BioSyst., 2011, 7, 1883 DOI: 10.1039/C1MB05008G

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