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Molecules 2018, 23(2), 249; https://doi.org/10.3390/molecules23020249

Interaction between Saikosaponin D, Paeoniflorin, and Human Serum Albumin

1
Department of Pathophysiology, Key Immunopharmacology Laboratory, 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.
Received: 23 December 2017 / Revised: 19 January 2018 / Accepted: 22 January 2018 / Published: 27 January 2018
(This article belongs to the Collection Herbal Medicine Research)
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Abstract

Saikosaponin D (SSD) and paeoniflorin (PF) are the major active constituents of Bupleuri Radix and Paeonia lactiflora Pall, respectively, and have been widely used in China to treat liver and other diseases for many centuries. We explored the binding of SSD/PF to human serum albumin (HSA) by using fluorospectrophotometry, circular dichroism (CD) and molecular docking. Both SSD and PF produced a conformational change in HSA. Fluorescence quenching was accompanied by a blue shift in the fluorescence spectra. Co-binding of PF and SSD also induced quenching and a conformational change in HSA. The Stern-Volmer equation showed that quenching was dominated by static quenching. The binding constant for ternary interaction was below that for binary interaction. Site-competitive experiments demonstrated that SSD/PF 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 the binary association. Also, there was energy transfer upon binary interaction. Molecular docking supported the experimental findings in conformation, binding sites and binding forces. View Full-Text
Keywords: saikosaponin; paeoniflorin; human serum albumin; spectroscopy; molecular docking saikosaponin; paeoniflorin; human serum albumin; spectroscopy; molecular docking
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).
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Liang, G.-W.; Chen, Y.-C.; Wang, Y.; Wang, H.-M.; Pan, X.-Y.; Chen, P.-H.; Niu, Q.-X. Interaction between Saikosaponin D, Paeoniflorin, and Human Serum Albumin. Molecules 2018, 23, 249.

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