کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5402194 | 1392728 | 2011 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Study on the interaction between promethazine hydrochloride and bovine serum albumin by fluorescence spectroscopy
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی تئوریک و عملی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The interaction between promethazine hydrochloride (PMT) and bovine serum albumin (BSA) in vitro was investigated by means of fluorescence spectroscopy and absorption spectroscopy. The fluorescence of BSA was quenched remarkably by PMT and the quenching mechanism was considered as static quenching by forming a complex. The association constants Ka and the number of binding sites n were calculated at different temperatures. The BSA-PMT binding distance was determined to be less than 8Â nm, suggesting that energy transfer from BSA to PMT may occur. The thermodynamic parameters of the interaction between PMT and BSA were measured according to the van't Hoff equation. The enthalpy change (ÎH) and entropy change (ÎS) were calculated to be â23.62Â kJÂ molâ1 and â0.10Â JÂ molâ1Â Kâ1, respectively, which indicated that the interaction of PMT with BSA was driven mainly by van der Waals forces and hydrogen bonds. The binding process was a spontaneous process in which Gibbs free energy change (ÎG) was negative. In addition, the results of synchronous fluorescence spectra and three-dimensional fluorescence spectra showed that binding of PMT with BSA can induce conformational changes in BSA.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Luminescence - Volume 131, Issue 2, February 2011, Pages 285-290
Journal: Journal of Luminescence - Volume 131, Issue 2, February 2011, Pages 285-290
نویسندگان
Lingling He, Xin Wang, Bin Liu, Jun Wang, Yaguang Sun, Enjun Gao, Shukun Xu,