title: Spectroscopic investigations on the binding of Pyronin Y to human serum albumin.
abstract: The interaction of Pyronin Y with human serum albumin (HSA) has been investigated systematically by fluorescence, absorption, fluorescence decay lifetime measurements, FTIR, synchronous fluorescence spectroscopy, and molecular modeling method. The spectroscopic and fluorescence quenching experiments show that Pyronin Y may show a static quenching mechanism with HSA. The specific binding distance of 1.96 nm between HSA and Pyronin Y was obtained via Förster non-radiation energy transfer method. The thermodynamic parameters indicate that the electrostatic interactions play a significant role during the binding process. In addition, synchronous fluorescence and FT-IR spectra indicated that the conformation and microenvironment of HSA were not influenced with the addition of Pyronin Y. The obtained results can be of biological significance in photodynamic therapy.
authors.affiliation: a Department of Chemistry , Bingol University , Bingöl 12000 , Turkey.
authors.forename: Abdullah
authors.initials: A
authors.lastname: Salci
authors.affiliation: a Department of Chemistry , Bingol University , Bingöl 12000 , Turkey.
authors.forename: Mahmut
authors.initials: M
authors.lastname: Toprak
mesh_terms: D001665:Binding Sites; D006801:Humans; D008968:Molecular Conformation; D062105:Molecular Docking Simulation; D056004:Molecular Dynamics Simulation; D011485:Protein Binding; D011754:Pyronine / Q000737:chemistry* / Q000378:metabolism; D012709:Serum Albumin / Q000737:chemistry* / Q000378:metabolism; D013050:Spectrometry, Fluorescence; D017550:Spectroscopy, Fourier Transform Infrared; D013057:Spectrum Analysis; D013816:Thermodynamics
chemical_list: D012709:Serum Albumin; D011754:Pyronine
keywords: HSA; Pyronin Y; fluorescence quenching; photodynamic