4.7 Article

Spectroscopy Study on the Interaction of Quercetin with Collagen

Journal

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 57, Issue 9, Pages 3431-3435

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/jf803671s

Keywords

Quercetin; collagen; fluorescence; quenching; spectroscopy; interaction

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In order to understand the interaction between quercetin and collagen clearly, the UV-vis, FTIR-HATR, and fluorescence spectroscopy were used, and the data obtained by these experiments suggested that quercetin could bind to collagen. Results of FTIR-HATR and UV-vis absorption spectra suggested that the interaction of quercetin and collagen did not alter the conformation of collagen. The fluorescence spectra revealed that collagen could cause the quenching of quercetin fluorescence through a dynamic quenching procedure. The calculated quenching constant K-SV and bimolecular quenching rate constant k(q) suggested that diffusion played a major role in quenching. In addition, the interaction of quercetin and collagen was evaluated by calculating (determining) the number of binding sites (n) and apparent binding constant K-A.

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