Multi-spectroscopic studies on the interaction between traditional Chinese herb, helicid with pepsin

Molecular Biology Reports
Manjunath D MetiHong Xu

Abstract

Study on the binding properties of helicid by pepsin systematically using multi-spectroscopic techniques and molecular docking method, and these interactions comprise biological recognition at molecular level and backbone of biological significance in medicine concerned with the uses, effects, and modes of action of drugs. We investigated the mechanism of interaction between helicid and pepsin by using various spectroscopic techniques viz., fluorescence spectra, UV-Vis absorption spectra, circular dichroism (CD), 3D spectra, synchronous fluorescence spectra and molecular docking methods. The quenching mechanism associated with the helicid-pepsin interaction was determined by performing fluorescence measurements at different temperatures. From the experimental results show that helicid quenched the fluorescence intensity of pepsin via a combination of static and dynamic quenching process. The binding constants (Ka) at three temperatures (288, 298, and 308 K) were 7.940 × 107, 2.082 × 105 and 3.199 × 105 L mol-1, respectively, and the number of binding sites (n) were 1.44, 1.14, and 1.18, respectively. The n value is close to unity, which means that there is only one independent class of binding site on pepsin for helicid. Thermo...Continue Reading

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Citations

May 6, 2021·Luminescence : the Journal of Biological and Chemical Luminescence·Yanzhou TaoLi Li

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Methods Mentioned

BETA
circular dichroism
fluorescence studies
fluorescence spectroscopy
protein folding

Software Mentioned

Surflex
MOE
Sybyl
DICHRO WEB
Dock

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