Interaction between Saikosaponin D, Paeoniflorin, and Human Serum Albumin

Autor: Qing-Xia Niu, Yi Wang, Guo-Wu Liang, Xiang-Yu Pan, Pei-Hong Chen, Yicun Chen, Hong-Mei Wang
Rok vydání: 2018
Předmět:
Protein Conformation
alpha-Helical
0301 basic medicine
Conformational change
Circular dichroism
Pharmaceutical Science
Paeonia
01 natural sciences
Analytical Chemistry
paeoniflorin
chemistry.chemical_compound
Glucosides
Drug Discovery
saikosaponin
human serum albumin
spectroscopy
molecular docking
Hydrogen bond
Human serum albumin
Molecular Docking Simulation
Chemistry (miscellaneous)
symbols
Thermodynamics
Molecular Medicine
van der Waals force
Protein Binding
medicine.drug
Serum Albumin
Human
Article
03 medical and health sciences
symbols.namesake
medicine
Humans
Protein Interaction Domains and Motifs
Oleanolic Acid
Physical and Theoretical Chemistry
Binding Sites
Quenching (fluorescence)
Plant Extracts
010405 organic chemistry
Organic Chemistry
Hydrogen Bonding
Saponins
Paeoniflorin
Binding constant
Bupleurum
0104 chemical sciences
Kinetics
Crystallography
030104 developmental biology
chemistry
Monoterpenes
Drugs
Chinese Herbal
Zdroj: Molecules; Volume 23; Issue 2; Pages: 249
Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry
ISSN: 1420-3049
DOI: 10.3390/molecules23020249
Popis: 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.
Databáze: OpenAIRE
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