title: Study on the interaction of antiviral drug 'Tenofovir' with human serum albumin by spectral and molecular modeling methods.
abstract: This study was designed to examine the interaction of Tenofovir (Ten) with human serum albumin (HSA) under physiological conditions. The binding of drugs with human serum albumin is a crucial factor influencing the distribution and bioactivity of drugs in the body. To understand the action mechanisms between Ten and HSA, the binding of Ten with HSA was investigated by a combined experimental and computational approach. UV-vis results confirmed that Ten interacted with HSA to form a ground-state complex and values of the Stern-Volmer quenching constant indicate the presence of a static component in the quenching mechanism. As indicated by the thermodynamic parameters (positive ΔH and ΔS values), hydrophobic interaction plays a major role in the Ten-HSA complex. Through the site marker competitive experiment, Ten was confirmed to be located in site I of HSA. Furthermore, UV-vis absorption spectra, synchronous fluorescence spectrum and CD data were used to investigate the structural change of HSA molecules with addition of Ten, the results indicate that the secondary structure of HSA molecules was changed in the presence of Ten. The experimental results were in agreement with the results obtained via molecular docking study.
authors.affiliation: Inorganic Chemistry Department, Faculty of Chemistry, Razi University, Kermanshah, Iran. Electronic address: NahidShahabadi@yahoo.com.
authors.forename: Nahid
authors.initials: N
authors.lastname: Shahabadi
authors.affiliation: Inorganic Chemistry Department, Faculty of Chemistry, Razi University, Kermanshah, Iran.
authors.forename: Saba
authors.initials: S
authors.lastname: Hadidi
authors.affiliation: Department of Chemistry, Semnan University, Semnan 425789-235, Iran.
authors.forename: Foroozan
authors.initials: F
authors.lastname: Feizi
mesh_terms: D000998:Antiviral Agents / Q000737:chemistry*; D001665:Binding Sites; D002942:Circular Dichroism; D003198:Computer Simulation; D006801:Humans; D007700:Kinetics; D062105:Molecular Docking Simulation; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012709:Serum Albumin / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D000068698:Tenofovir / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D000998:Antiviral Agents; D012709:Serum Albumin; D000068698:Tenofovir
keywords: Drug–protein interaction; Experimental and computational approach; Human serum albumin; Tenofovir