کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5402377 | 1392732 | 2010 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Spectroscopic investigation of the interaction between thiourea-zinc complex and serum albumin
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موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی تئوریک و عملی
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چکیده انگلیسی
The interaction between 1-Zn (N-p-(dimethylamino)benzamido-Nâ²-phenylthiourea-zinc) complex and serum albumins was studied. In the presence of proteins such as BSA or HSA, the fluorescence spectrum of 1 did not change. However, the fluorescence intensity of its zinc complex (1-Zn) was greatly enhanced. It was ascribed to the fact that zinc ion promoted the interaction between 1 and proteins. Therefore, it was concluded that zinc ion could facilitate bioactivity of thiourea derivative drugs. Energy transfer occurred between 1-Zn and the proteins, which led to decrease of proteins' emission and increase of 1-Zn's emission. The fluorescence quenching of serum albumins by 1-Zn was considered as a static quenching process. The binding constants between 1-Zn and serum albumins were estimated as 1.02Ã1012Â molâ1Â L for BSA and 1.32Ã1010Â molâ1Â L for HSA, respectively, and the number of binding sites was 2 for both. The effect of 1-Zn on the conformation of serum albumins was further investigated using synchronous fluorescence spectrometry and the results implied that tyrosine residues of proteins were closer to 1-Zn than tryptophan residues.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Luminescence - Volume 130, Issue 7, July 2010, Pages 1280-1284
Journal: Journal of Luminescence - Volume 130, Issue 7, July 2010, Pages 1280-1284
نویسندگان
Fang-Ying Wu, Li-Na Zhang, Zhao-Jun Ji, Xiao-Fen Wan,