The interaction of 2-mercaptobenzimidazole with human serum albumin as determined by spectroscopy, atomic force microscopy and molecular modeling

• Published in: Colloids and surfaces, B, Biointerfaces B, Biointerfaces, 2013-04, Vol.104, p.311-317
• Main Authors: Li, Yuqin, Jia, Baoxiu, Wang, Hao, Li, Nana, Chen, Gaopan, Lin, Yuejuan, Gao, Wenhua
• Format: Article
• Language: English
• Subjects: 2-Mercaptobenzimidazole; amino acids; Atomic force microscopy; Benzimidazoles - chemistry; binding sites; Circular Dichroism; colloids; dialysis; energy transfer; fluorescence; Fluorescence spectra; Fourier transform infrared; Fourier transform infrared spectroscopy; Human serum albumin; Humans; hydrophobic bonding; hydrophobicity; in vitro studies; Microscopy, Atomic Force; Models, Molecular; Molecular modeling; molecular models; Raman spectra; Raman spectroscopy; Serum Albumin - chemistry; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis, Raman; temperature; thermodynamics; ultraviolet-visible spectroscopy; UV–vis
• ISSN: 0927-7765; 1873-4367
• DOI: 10.1016/j.colsurfb.2012.12.023

[Display omitted] ► The interaction of 2-mercaptobenzimidazole (MBI) with HSA studied in vitro by molecule modeling. ► The interaction of MBI with HSA studied in vitro by atomic force microscopy, CD, FTIR and Raman spectra. ► Steady state and time resolved fluorescence spectroscopy suggested that the quenching mechanism was dynamic. ► The binding parameters were determined according to the Stern–Volmer equation. ► The thermodynamic results indicated that hydrophobic interaction was the predominant force. The interaction of 2-mercaptobenzimidazole (MBI) with human serum albumin (HSA) was studied in vitro by equilibrium dialysis under normal physiological conditions. This study used fluorescence, ultraviolet–visible spectroscopy (UV–vis), Fourier transform infrared (FT-IR), circular dichroism (CD) and Raman spectroscopy, atomic force microscopy (AFM) and molecular modeling techniques. Association constants, the number of binding sites and basic thermodynamic parameters were used to investigate the quenching mechanism. Based on the fluorescence resonance energy transfer, the distance between the HSA and MBI was 2.495nm. The ΔG0, ΔH0, and ΔS0 values across temperature indicated that the hydrophobic interaction was the predominant binding Force. The UV, FT-IR, CD and Raman spectra confirmed that the HSA secondary structure was altered in the presence of MBI. In addition, the molecular modeling showed that the MBI–HSA complex was stabilized by hydrophobic forces, which resulted from amino acid residues. The AFM results revealed that the individual HSA molecule dimensions were larger after interaction with MBI. Overall, this study suggested a method for characterizing the weak intermolecular interaction. In addition, this method is potentially useful for elucidating the toxigenicity of MBI when it is combined with the biomolecular function effect, transmembrane transport, toxicological testing and other experiments.