title: Quenching of fluorescence by meclizine, a probe study for structural and conformational changes in human serum albumin.
abstract: The goal of this study was to investigate the interactions between meclizine (MEC) and human serum albumin (HSA) under physiological conditions by different spectroscopies and molecular modeling technique. The drug, MEC quenched the intrinsic fluorescence of HSA and the analysis of the results revealed that static quenching mechanism. The binding of MEC quenches the HSA fluorescence; stoichiometry was 1:1 interaction. Thermodynamic quantities were calculated at different temperatures suggested that hydrophobic and van der Waals interaction with HSA-MEC. The molecular distance, r, between donor and acceptor was estimated according to Forster's theory of non-radiation energy transfer. CD and FT-IR studies confirm changes of secondary structure of HSA. Molecular docking studies validate MEC molecule interact to HSA in sub domain IIA.
authors: a Department of Studies in Chemistry , Karnatak University , Dharwad 580003 , India.
authors: Girish G
authors: GG
authors: Ariga
authors: a Department of Studies in Chemistry , Karnatak University , Dharwad 580003 , India.
authors: Praveen N
authors: PN
authors: Naik
authors: a Department of Studies in Chemistry , Karnatak University , Dharwad 580003 , India.
authors: Sharanappa T
authors: ST
authors: Nandibewoor
authors: a Department of Studies in Chemistry , Karnatak University , Dharwad 580003 , India.
authors: Shivamurti A
authors: http://orcid.org/0000-0001-5382-7317
authors: SA
authors: Chimatadar
mesh_terms: D001665:Binding Sites; D002942:Circular Dichroism; D006801:Humans; D008024:Ligands; D008468:Meclizine / Q000737:chemistry*; D008958:Models, Molecular; D008968:Molecular Conformation; D011485:Protein Binding; D000075462:Serum Albumin, Human / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D017550:Spectroscopy, Fourier Transform Infrared; D013816:Thermodynamics
chemical_list: D008024:Ligands; D008468:Meclizine; D000075462:Serum Albumin, Human
keywords: Forster’s energy transfer; circular dichroism; human serum albumin; meclizine; molecular docking