پديدآورندگان :
Dezhampanah Hamid h.dpanah@guilan.ac.ir Department of Chemistry, Faculty of Science, University of Guilan, Rasht, Iran; , Akbarnia Dafrazi Atefe atefe.aka@gmail.com Department of Chemistry, Faculty of Science, University of Guilan, Rasht, Iran; , Ghanadzadeh Gilani Ali aggilani@gmail.com Department of Chemistry, Faculty of Science, University of Guilan, Rasht, Iran;
كليدواژه :
fluorescence resonance energy transfer , fluorescence spectroscopy , Uv , vis absorption
چكيده فارسي :
The intraction of 2- methyl -3-((1, 2- methyl-1H- indol-3- yl)((2- nitrophenyl) methyl) indole dye (BIM) with bovine serum albumin (BSA) in the pH range 5-8.5 was investigated using Uv-vis absorption, fluorescence spectroscopy and molecular docking calculations. The results showed that the fluorescence of BSA was quenched by BSA. The fluorescence quenching measurements revealed the presence of a single binding site on BSA for BIM with the bindi constant value equals to 4.40 *104 M-1. The result of Uv-vis revealed at the different pH buffer solution that binding affinities of BIM to BSA in the pH=5 was higher than other conditions values. The Molecular docking results indicated that BIM could strongly bind to the site I (subdomain IIA) of BSA mainly by hydrophobic interaction and there were hydrogen bond interactions between BIM and BSA. Hydrophobic interactions and hydrogen bond were the predominant intermolecular forces in stabilizing the BIM-BSA complex. The distance between donor and acceptor, obtained according to fluorescence resonance energy transfer (FRET) and docking studies, indicated that the BIM had hydrophobicity around the Trp residues of BSA and transferred to an aqueous or hydrophilic environment.
