Exploring the interaction of the photodynamic therapeutic agent thionine with bovine serum albumin: multispectroscopic and molecular docking studies
作者： Perumal Manivel , Shanmugam Anandakumar , Malaichamy Ilanchelian
DOI: 10.1002/BIO.2812
关键词: Quenching (fluorescence) 、 Bovine serum albumin 、 Chemistry 、 Emission spectrum 、 Biophysics 、 Thionine 、 Stereochemistry 、 Circular dichroism 、 Binding site 、 Protein secondary structure 、 Binding constant
摘要: This study explores the binding interaction of thionine (TH) with bovine serum albumin (BSA) under physiological conditions (pH 7.40) using absorption, emission, synchronous circular dichroism (CD) and three-dimensional (3D) emission spectral studies. The results titration experiments revealed that TH strongly quenches intrinsic BSA via a static quenching mechanism. apparent constant (K) number sites (n) were calculated as 2.09 × 105 dm3/mol n~1, respectively. negative free energy change value for BSA–TH system suggested was spontaneous energetically favourable. from CD 3D studies demonstrated induces changes in microenvironment secondary structure BSA. Site marker competitive site located subdomain IIA (Sudlow I) molecular docking further substantiates Sudlow I preferable Copyright © 2014 John Wiley & Sons, Ltd.
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