Department of Chemistry, University of Mysore, Manasagangothri, Mysuru 570 006, Karnataka, India.
Department of Chemistry, University of Mysore, Manasagangothri, Mysuru 570 006, Karnataka, India.
Spectrochim Acta A Mol Biomol Spectrosc. 2019 Feb 15;209:264-273. doi: 10.1016/j.saa.2018.10.047. Epub 2018 Oct 29.
Bupropion hydrochloride (BPH) an antidepressant and widely used to treat addiction of nicotine. The actual protein existing in blood plasma for the vehicle of exogenous and endogenous substances is human serum albumin i.e. HSA. The interaction of BPH with HSA was examined by molecular docking, multiple spectroscopy's such as fluorescence (emission, synchronous and three-dimensional), UV-vis (ultraviolet-visible), FT-IR (Fourier transform infrared) and CD (circular dichroism) at physiological pH 7.40 at 286, 296 and 306 K. BPH was particularly bind to HSA through forces called hydrogen bonds and vander Waals at site I (IIA) which was confirmed from negative values of thermodynamics calculated by van't Hoff equation and docking studies in addition to site marker analysis. This interaction was spontaneous and exothermic process. Secondary structure including conformation of HSA changes after interaction with BPH was revealed from CD and FT-IR (Fourier self-deconvolution to curve fitting), UV-vis, 3D and synchronous florescence techniques. Forster's theory (non-radiation energy transfer) was applied to calculate the distance from tryptophan of HSA to BPH. This interaction involves static quenching (Stern-Volmer and Modified Stern-Volmer equations) with larger binding constant values were in the range 10 confirming that strong interaction was exists between BPH and HSA. The interference of bio-active Mg, Cu, Zn, Ca and Fe metal ions on this interaction was also analysed.
盐酸安非他酮（BPH）是一种抗抑郁药，广泛用于治疗尼古丁成瘾。在血液血浆中，实际存在的蛋白质是作为外源性和内源性物质载体的人血清白蛋白，即 HSA。通过分子对接、多种光谱技术，如荧光（发射、同步和三维）、紫外可见（UV-可见）、傅里叶变换红外（FT-IR）和圆二色性（CD），在生理 pH 值 7.40 下，在 286、296 和 306 K 下研究了 BPH 与人血清白蛋白的相互作用。BPH 通过氢键和范德华力特别结合到 HSA 上，这一点通过 van't Hoff 方程和对接研究计算的热力学负值以及位点标记分析得到了证实。这种相互作用是自发的和放热的过程。BPH 与人血清白蛋白相互作用后，二级结构（包括 HSA 的构象）的变化通过 CD 和 FT-IR（傅里叶自解卷积到曲线拟合）、UV-可见、3D 和同步荧光技术揭示。福斯特理论（非辐射能量转移）被应用于计算 HSA 中色氨酸与 BPH 之间的距离。这种相互作用涉及静态猝灭（Stern-Volmer 和 Modified Stern-Volmer 方程），较大的结合常数值在 10 的范围内，这表明 BPH 和 HSA 之间存在强烈的相互作用。还分析了生物活性 Mg、Cu、Zn、Ca 和 Fe 金属离子对这种相互作用的干扰。
