Journal
JOURNAL OF MOLECULAR STRUCTURE
Volume 921, Issue 1-3, Pages 188-198Publisher
ELSEVIER
DOI: 10.1016/j.molstruc.2008.12.047
Keywords
Human serum albumin; Fluorescence quenching; Two-dimensional fluorescence correlation analysis; CD; FT-IR; Molecular modeling
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The binding of a novel carditionic agent (2-amino-4-chloro-N-(4-(6-oxo-1,4,5,6-tetrahydropyridazin-3yl)phenyl)benzamide (ACPB)) to human serum albumin (HSA) under physiological conditions has been investigated by using UV/vis absorption, fluorescence, circular dichroism (CD) and Fourier transform infrared (FT-IR) in combination with protein-ligand docking study. It was observed that there was a prominent interaction between ACPB and HSA. The interaction was also confirmed by two-dimensional (2D) correction analysis based on the quenching perturbation on the fluorescence spectra and the order of the response of ACPB and HSA to the quenching perturbation was also elucidated based on Noda's rule. Fluorescence data revealed that the fluorescence quenching was a static quenching process and the binding constants were calculated to be 8.781 x 10(5), 7.310 x 10(5), and 5.358 x 10(5) M-1 at 290, 300, and 310 K, respectively. The thermodynamic parameters were calculated according to the Van't Hoff equation and the binding mode was determined. In addition, the alterations of protein secondary structure were qualitatively and quantitatively determined by the evidence from synchronous fluorescence, CD and FT-IR. Furthermore, docking studies that corroborate our experimental results revealed that the binding sites were located in subdomain IIA of HSA. (C) 2008 Elsevier B.V. All rights reserved.
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