Interaction between saikosaponin D, paeoniflorin, and human serum albumin.
作者： Guo-Wu Liang , Yi-Cun Chen , Yi Wang , Hong-Mei Wang , Xiang-Yu Pan
DOI: 10.3390/MOLECULES23020249
关键词:
摘要: Saikosaponin D (SSD) and paeoniflorin (PF) are the major active constituents of Bupleuri Radix Paeonia lactiflora Pall, respectively, have been widely used in China to treat liver other diseases for many centuries. We explored binding SSD/PF human serum albumin (HSA) by using fluorospectrophotometry, circular dichroism (CD) molecular docking. Both SSD PF produced a conformational change HSA. Fluorescence quenching was accompanied blue shift fluorescence spectra. Co-binding also induced The Stern-Volmer equation showed that dominated static quenching. constant ternary interaction below binary interaction. Site-competitive experiments demonstrated bound site I (subdomain IIA) II IIIA) Analysis thermodynamic parameters indicated hydrogen bonding van der Waals forces were mostly responsible association. Also, there energy transfer upon Molecular docking supported experimental findings conformation, sites forces.
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