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Molecules 2016, 21(2), 153; doi:10.3390/molecules21020153

Binding between Saikosaponin C and Human Serum Albumin by Fluorescence Spectroscopy and Molecular Docking

1
Key Immunopharmacology Laboratory of Guangdong Province, Department of Pathophysiology, Institute of Inflammation and Immune Diseases, Shantou University Medical College, Guangdong 515041, China
2
Department of Pharmacology, Traditional Chinese Medicine Laboratory, Shantou University Medical College, Guangdong 515041, China
These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
Academic Editor: Derek J. McPhee
Received: 11 November 2015 / Revised: 18 January 2016 / Accepted: 21 January 2016 / Published: 28 January 2016
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Abstract

Saikosaponin C (SSC) is one of the major active constituents of dried Radix bupleuri root (Chaihu in Chinese) that has been widely used in China to treat a variety of conditions, such as liver disease, for many centuries. The binding of SSC to human serum albumin (HSA) was explored by fluorescence, circular dichroism (CD), UV-vis spectrophotometry, and molecular docking to understand both the pharmacology and the basis of the clinical use of SSC/Chaihu. SSC produced a concentration-dependent quenching effect on the intrinsic fluorescence of HSA, accompanied by a blue shift in the fluorescence spectra. The Stern-Volmer equation showed that this quenching was dominated by static quenching. The binding constant of SSC with HSA was 3.72 × 103 and 2.99 × 103 L·mol−1 at 26 °C and 36 °C, respectively, with a single binding site on each SSC and HSA molecule. Site competitive experiments demonstrated that SSC bound to site I (subdomain IIA) and site II (subdomain IIIA) in HSA. Analysis of thermodynamic parameters indicated that hydrogen bonding and van der Waals forces were mostly responsible for SSC-HSA association. The energy transfer efficiency and binding distance between SSC and HSA was calculated to be 0.23 J and 2.61 nm at 26 °C, respectively. Synchronous fluorescence and CD measurements indicated that SSC affected HSA conformation in the SSC-HSA complex. Molecular docking supported the experimental findings in conformational changes, binding sites and binding forces, and revealed binding of SSC at the interface between subdomains IIA-IIB. View Full-Text
Keywords: saikosaponin C; human serum albumin; static quenching; Radix bupleuri; molecular docking; Chaihu saikosaponin C; human serum albumin; static quenching; Radix bupleuri; molecular docking; Chaihu
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MDPI and ACS Style

Chen, Y.-C.; Wang, H.-M.; Niu, Q.-X.; Ye, D.-Y.; Liang, G.-W. Binding between Saikosaponin C and Human Serum Albumin by Fluorescence Spectroscopy and Molecular Docking. Molecules 2016, 21, 153.

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