کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1229978 1495198 2017 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Biophysical influence of coumarin 35 on bovine serum albumin: Spectroscopic study
ترجمه فارسی عنوان
نفوذ بیوفیزیکی از کومارین 35 در آلبومین سرم گاوی: مطالعه طیف
کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی آنالیزی یا شیمی تجزیه
چکیده انگلیسی


• Interaction of bovine serum albumin (BSA) with coumarin 35 (C35) were spectroscopically examined.
• A fluorescence quenching process for BSA-C35 system was occurred.
• The synchronize fluorescence studies showed that C35 molecules approached to BSA by its tyrosine region.

The binding mechanism and protein–fluorescence probe interactions between bovine serum albumin (BSA) and coumarin 35 (C35) was investigated by using UV–Vis absorption and fluorescence spectroscopies since they remain major research topics in biophysics. The spectroscopic data indicated that a fluorescence quenching process for BSA–C35 system was occurred. The fluorescence quenching processes were analyzed using Stern-Volmer method. In this regard, Stern-Volmer quenching constants (KSV) and binding constants were calculated at different temperatures. The distance r between BSA (donor) and C35 (acceptor) was determined by exploiting fluorescence resonance energy transfer (FRET) method. Synchronous fluorescence spectra were also studied to observe information about conformational changes. Moreover, thermodynamics parameters were calculated for better understanding of interactions and conformational changes of the system.

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ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy - Volume 171, 15 January 2017, Pages 90–96
نویسندگان
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