کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1410343 1501867 2009 11 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Studies on the binding of a carditionic agent to human serum albumin by two-dimensional correlation fluorescence spectroscopy and molecular modeling
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی آلی
پیش نمایش صفحه اول مقاله
Studies on the binding of a carditionic agent to human serum albumin by two-dimensional correlation fluorescence spectroscopy and molecular modeling
چکیده انگلیسی

The binding of a novel carditionic agent (2-amino-4-chloro-N-(4-(6-oxo-1,4,5,6-tetrahydropyridazin-3-yl)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 × 105, 7.310 × 105, and 5.358 × 105 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.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Molecular Structure - Volume 921, Issues 1–3, 17 March 2009, Pages 188–198
نویسندگان
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