title: Biophysical and molecular docking approaches for the investigation of biomolecular interactions between amphotericin B and bovine serum albumin.
abstract: Exogenous drug as an antidote to treat various infections get absorbed in the blood circulatory system of a human can directly contact with transporter proteins such as serum albumin. Therefore, for rational drug discovery, understanding the biomolecular interaction between drugs and protein is highly important. In this contribution, we describe the possible interactions between an antifungal drug Amphotericin B (AmB) and Bovine Serum Albumin (BSA) using multi-spectroscopic techniques and further confirmed through in-silico approaches. Binding effects of AmB on BSA conformation, surface morphology, topology, and stability were determined by Ultraviolet-visible spectroscopy (UV), Fourier transform infrared spectroscopy (FT-IR), Circular Dichroism (CD), Transmission Electron Microscopy (TEM), Dynamic Light Scattering (DLS), Fluorescence Spectroscopy and Molecular dynamic simulations. The Stern-Volmer equation was used to determine the binding site (0.4) and binding constant (8.16×105M-1). The intrinsic intensity of the native BSA was quenched by AmB through static quenching mechanism. The calculated Gibbs free energy value (-8.70kcal/mol) indicated the involvement of hydrogen bonding and hydrophobic contacts in BSA-AmB interaction. The hydrodynamic radii and surface contact area of BSA-AmB molecules are decreasing which can strongly support the stabilizing action of complex particles. Moreover, the finding of this work will provide information for the drug designers to further study the AmB binding mechanism and their pharmacodynamics and pharmacokinetics features in order to achieve better therapeutic efficacy.
authors.affiliation: State Key Laboratory of Chemical Resource Engineering, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, PR China; Beijing Key Lab of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, 15 Bei San Huan East Road, P. O. Box 53, Beijing 100029, PR China.
authors.forename: Muslim
authors.initials: M
authors.lastname: Raza
authors.affiliation: State Key Laboratory of Chemical Resource Engineering, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, PR China.
authors.forename: Aftab
authors.initials: A
authors.lastname: Ahmad
authors.affiliation: Beijing Key Lab of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, 15 Bei San Huan East Road, P. O. Box 53, Beijing 100029, PR China.
authors.forename: Feng
authors.initials: F
authors.lastname: Yue
authors.affiliation: Institute of Chemical Sciences, Biochemistry Section, University of Peshawar, 25120, Pakistan.
authors.forename: Zahid
authors.initials: Z
authors.lastname: Khan
authors.affiliation: Beijing Key Lab of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, 15 Bei San Huan East Road, P. O. Box 53, Beijing 100029, PR China.
authors.forename: Yang
authors.initials: Y
authors.lastname: Jiang
authors.affiliation: State Key Laboratory of Chemical Resource Engineering, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, PR China.
authors.forename: Yun
authors.initials: Y
authors.lastname: Wei
authors.affiliation: State Key Laboratory of Chemical Resource Engineering, College of Materials Science and Engineering, Beijing University of Chemical Technology, Beijing 100029, PR China.
authors.forename: Saleem
authors.initials: S
authors.lastname: Raza
authors.affiliation: Beijing Key Lab of Bioprocess, College of Life Science and Technology, Beijing University of Chemical Technology, 15 Bei San Huan East Road, P. O. Box 53, Beijing 100029, PR China.
authors.forename: Wang Wen
authors.initials: WW
authors.lastname: He
authors.affiliation: State Key Laboratory of Chemical Resource Engineering, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, PR China.
authors.forename: Faheem Ullah
authors.initials: FU
authors.lastname: Khan
authors.affiliation: State Key Laboratory of Chemical Resource Engineering, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, PR China. Electronic address: yuanqp@mail.buct.edu.cn.
authors.forename: Yuan
authors.initials: Y
authors.lastname: Qipeng
mesh_terms: D000666:Amphotericin B / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002942:Circular Dichroism; D000067493:Dynamic Light Scattering; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D046529:Microscopy, Electron, Transmission; D062105:Molecular Docking Simulation; D017434:Protein Structure, Tertiary; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: D012710:Serum Albumin, Bovine; D000666:Amphotericin B
keywords: Amphotericin B; Biomolecular interaction; Bovine serum albumin; Molecular docking; Molecular dynamics simulation; Spectroscopy