title: Binding and conformational changes of human serum albumin upon interaction with 4-aminoantipyrine studied by spectroscopic methods and cyclic voltammetry.
abstract: The interactions of 4-aminoantipyrine (AAP) with human serum albumin (HSA) have been studied by UV-visible spectroscopy, fluorescence spectroscopy and cyclic voltammetry. The binding of 4-aminoantipyrine quenches the HSA fluorescence, revealing a 1:1 interaction with a binding constant of about 10(5) M(-1). The experimental results showed that AAP effectively quenched the intrinsic fluorescence of HSA via dynamic type of quenching. In addition, according to the synchronous fluorescence spectra of HSA in presence of 4-aminoantipyrine, the tryptophan residue of the proteins are most perturbed by the binding process. The number of binding sites, the binding constant, site probe study, some common metal ions effect and the thermodynamic parameters were calculated.
authors: P.G. Department of Studies in Chemistry, Karnatak University, Dharwad 580 003, India.
authors: Jayant I
authors: JI
authors: Gowda
authors: P.G. Department of Studies in Chemistry, Karnatak University, Dharwad 580 003, India. Electronic address: stnandibewoor@yahoo.com.
authors: Sharanappa T
authors: ST
authors: Nandibewoor
mesh_terms: D065966:Absorption, Physicochemical; D000675:Ampyrone / Q000737:chemistry / Q000378:metabolism*; D002942:Circular Dichroism; D055664:Electrochemical Techniques / Q000379:methods*; D006801:Humans; D007477:Ions; D007700:Kinetics; D008670:Metals / Q000737:chemistry; D011485:Protein Binding; D011487:Protein Conformation; D012709:Serum Albumin / Q000737:chemistry* / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D017550:Spectroscopy, Fourier Transform Infrared; D013057:Spectrum Analysis; D013696:Temperature
chemical_list: D007477:Ions; D008670:Metals; D012709:Serum Albumin; D000675:Ampyrone
keywords: 4-Aminoantipyrine; Binding constant; Human serum albumin; Spectroscopy; Thermodynamic parameter