کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1234268 1495244 2014 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Investigation of interaction of antibacterial drug sulfamethoxazole with human serum albumin by molecular modeling and multi-spectroscopic method
ترجمه فارسی عنوان
بررسی اثر متقابل سولفامتوکسازول داروی ضد باکتری با آلبومین سرم انسان با استفاده از مدل سازی مولکولی و روش چند اسپکتروسکوپی
کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی آنالیزی یا شیمی تجزیه
چکیده انگلیسی


• The interaction of SMX and HSA was firstly predicted through molecular modeling.
• The binding parameters were performed through the fluorescence quenching spectra.
• The thermodynamic parameters were calculated by the Van’t Hoff equations.
• The conformational changes of HSA were confirmed by multi-spectroscopic methods.

Interaction of sulfamethoxazole (SMX) with human serum albumin (HSA) was investigated by molecular modeling and multi-spectroscopic methods under physiological conditions. The interaction mechanism was firstly predicted through molecular modeling that confirmed the interaction between SMX and HSA. The binding parameters and the thermodynamic parameters at different temperatures for the reaction had been calculated according to the Stern–Volmer, Hill, Scatchard and the Van’t Hoff equations, respectively. One independent class of binding site existed during the interaction between HSA and SMX. The binding constants decreased with the increasing temperatures, which meant that the quenching mechanism was a static quenching. The thermodynamic parameters of the reaction, namely standard enthalpy ΔH0 and entropy ΔS0, had been calculated to be −16.40 kJ mol−1 and 32.33 J mol−1 K−1, respectively, which suggested that the binding process was exothermic, enthalpy driven and spontaneous. SMX bound to HSA was mainly based on electrostatic interaction, but hydrophobic interactions and hydrogen bonds could not be excluded from the binding. The conformational changes of HSA in the presence of SMX were confirmed by the three-dimensional fluorescence spectroscopy, UV–vis absorption spectroscopy and circular dichroism (CD) spectroscopy. CD data suggested that the protein conformation was altered with the reduction of α-helices from 55.37% to 41.97% at molar ratio of SMX/HSA of 4:1.

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ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy - Volume 124, 24 April 2014, Pages 84–90
نویسندگان
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