کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1229050 1495231 2015 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Study on the interaction of antiviral drug ‘Tenofovir’ with human serum albumin by spectral and molecular modeling methods
ترجمه فارسی عنوان
مطالعه بر روی متابولیسم داروهای ضد ویروسی تنفوویرا با آلبومین سرم انسان با روش های مدل سازی طیفی و مولکولی
کلمات کلیدی
تنفوویر، آلبومین سرم انسان، متابولیسم پروتئین، رویکرد تجربی و محاسباتی
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی آنالیزی یا شیمی تجزیه
چکیده انگلیسی


• The mechanism of interaction was studied by spectroscopic techniques combination with molecular modeling.
• The UV–vis spectra and fluorescence quenching data indicated that Ten forms a complex with HSA in the ground state.
• Through the site marker competitive experiment, Ten was confirmed to be located in subdomain IIA of HSA.

This study was designed to examine the interaction of Tenofovir (Ten) with human serum albumin (HSA) under physiological conditions. The binding of drugs with human serum albumin is a crucial factor influencing the distribution and bioactivity of drugs in the body. To understand the action mechanisms between Ten and HSA, the binding of Ten with HSA was investigated by a combined experimental and computational approach. UV–vis results confirmed that Ten interacted with HSA to form a ground-state complex and values of the Stern–Volmer quenching constant indicate the presence of a static component in the quenching mechanism. As indicated by the thermodynamic parameters (positive ΔH and ΔS values), hydrophobic interaction plays a major role in the Ten–HSA complex. Through the site marker competitive experiment, Ten was confirmed to be located in site I of HSA. Furthermore, UV–vis absorption spectra, synchronous fluorescence spectrum and CD data were used to investigate the structural change of HSA molecules with addition of Ten, the results indicate that the secondary structure of HSA molecules was changed in the presence of Ten. The experimental results were in agreement with the results obtained via molecular docking study.

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ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy - Volume 138, 5 March 2015, Pages 169–175
نویسندگان
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