ArticleMolecules (Basel, Switzerland)2016
Binding between Saikosaponin C and Human Serum Albumin by Fluorescence Spectroscopy and Molecular Docking.
Article in Molecules (Basel, Switzerland), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 58 citations in OpenAlex.
- Unravelling the physicochemical and antimicrobial mechanisms of human serum albumin/tannic acid coatings for medical-grade polycaprolactone scaffolds.Bioactive materials · 2024Article
- Structural and in vitro anticancer properties of the kaempferol-lactoferrin complex.Food science & nutrition · 2024Article
- Insights into the binding of buspirone to human serum albumin using multi-spectroscopic and molecular docking techniques.Heliyon · 2024Article
- Molecular Dynamics and Multi-Spectroscopic of the Interaction Behavior between Bladder Cancer Cells and Calf Thymus DNA with Rebeccamycin: Apoptosis through the Down Regulation of PI3K/AKT Signaling Pathway.Journal of fluorescence · 2023Article
- Mode of binding, kinetic and thermodynamic properties of a lipid-like drug (Fingolimod) interacting with Human Serum Albumin.BioImpacts : BI · 2023Article
- Insight into the Interaction Mechanism of HSA with Aztreonam: A Multispectroscopic and Computational Approach.Molecules (Basel, Switzerland) · 2022Article
- Elucidation of the binding mechanism of astragaloside IV derivative with human serum albumin and its cardiotoxicity in zebrafish embryos.Frontiers in pharmacology · 2022Article
- Binding Studies of AICAR and Human Serum Albumin by Spectroscopic, Theoretical, and Computational Methodologies.Molecules (Basel, Switzerland) · 2020Article
- A Comprehensive Spectroscopic Analysis of the Ibuprofen Binding with Human Serum Albumin, Part I.Pharmaceuticals (Basel, Switzerland) · 2020Article
- α-Glucosidase inhibitors from Chinese bayberry (RSC advances · 2020Article
- Molecular dynamics simulation as a tool for assessment of drug binding property of human serum albumin.Molecular biology reports · 2018Article
- Oxidative Alteration of Trp-214 and Lys-199 in Human Serum Albumin Increases Binding Affinity with Phenylbutazone: A Combined Experimental and Computational Investigation.International journal of molecular sciences · 2018Article
- Interaction between Saikosaponin D, Paeoniflorin, and Human Serum Albumin.Molecules (Basel, Switzerland) · 2018Article
- Biointeractions of Herbicide Atrazine with Human Serum Albumin: UV-Vis, Fluorescence and Circular Dichroism Approaches.International journal of environmental research and public health · 2018Article
- A glucose/mannose binding lectin from litchi (Biochemistry and biophysics reports · 2016Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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