Spectroscopy study on the interaction of quercetin with collagen.
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).
Yang
Xiaozhan
X
Institute of Materia Medica, College of Pharmay, Third Military Medical University, Chongqing 400038, People's Republic of China.
Wu
Dacheng
D
Du
Zongliang
Z
Li
Ruixia
R
Chen
Xulong
X
Li
Xiaohui
X