Characterization of the interaction between 3-Oxotabersonine and two serum albumins by using spectroscopic techniques

• Published in: Journal of luminescence Vol. 138; pp. 1 - 7
• Main Authors: Wang, Qing, Yan, Jin, He, Jiawei, Bai, Keke, Li, Hui
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 01.06.2013; Elsevier
• Subjects: 3-Oxotabersonine; Binding; Binding sites; Bovine serum albumin (BSA); Cold working, work hardening; annealing, quenching, tempering, recovery, and recrystallization; textures; Condensed matter: electronic structure, electrical, magnetic, and optical properties; Condensed matter: structure, mechanical and thermal properties; Cross-disciplinary physics: materials science; rheology; Dichroism; Entropy; Exact sciences and technology; Human serum albumin (HSA); Interaction; Materials science; Mathematical models; Molecular modeling; Optical properties and condensed-matter spectroscopy and other interactions of matter with particles and radiation; Photoluminescence; Physics; Quenching; Serum albumin; Spectroscopy; Thermal properties of condensed matter; Thermal properties of crystalline solids; Thermodynamic properties; Treatment of materials and its effects on microstructure and properties; 3-Oxotabersonine; Bovine serum albumin (BSA); Human serum albumin (HSA); Interaction; Molecular modeling; Drugs; Cadmium; Fourier transformation; Phase transformations; Enthalpy; Fluorescence; Entropy; Infrared spectra; Circular dichroism; Diseases; Quenching; Albumins; Modelling; Man
• ISSN: 0022-2313; 1872-7883
• DOI: 10.1016/j.jlumin.2013.01.035

3-Oxotabersonine (OTAB) is a component of Voacanga africana, which is a type of traditional drug in Africa widely used for treating diseases. This study examines the interaction of OTAB with bovine serum albumin (BSA) and human serum albumin (HSA) under physiological conditions. The interaction between OTAB and BSA/HSA was investigated using fluorescence spectroscopy, Fourier transform infrared (FT-IR) spectroscopy, circular dichroism (CD) spectroscopy, and molecular modeling under simulated physiological conditions. The experimental results confirm that the quenching mechanism is a static quenching process. The binding site number (n) and the apparent binding constant (K) were measured at various temperatures. The thermodynamic parameters, namely, enthalpy change (ΔH) and entropy change (ΔS), were calculated. Furthermore, the structural changes in the serum albumin that affected the OTAB binding were determined using FT-IR. The binding site was assumed to be located in site I of the BSA/HSA (subdomain IIA). ► Make use of the 3-Oxotabersonine firstly extracted from seeds of Voacanga africana Stapf to study the drug–protein system. ► Use two kinds of similar structure serum albumins to do a comparative study. ► FT-IR was used to study the conformational change of BSA and HSA. ► Use the BSA and HSA structure obtained from the Brookhaven Protein Data Bank for molecular docking.