کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5403822 | 1392768 | 2008 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Interaction of nobiletin with human serum albumin studied using optical spectroscopy and molecular modeling methods
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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 binding of nobiletin to human serum albumin (HSA) was investigated by fluorescence, UV-vis, FT-IR, CD, and molecular modeling. Fluorescence data revealed the presence of a single class of binding site on HSA and its binding constants (K) at four different temperatures (289, 296, 303 and 310Â K) were 4.054, 4.769, 5.646 and 7.044Ã104Â Mâ1, respectively. The enthalpy change (ÎH0) and the entropy changes (ÎS0) were calculated to be 1.938Â kJÂ molâ1 and 155.195Â JÂ molâ1Â Kâ1 according to the Van't Hoff equation. The binding average distance, r, between the donor (HSA) and the acceptor (nobiletin) was evaluated and found to be 2.33Â nm according to the Förster's theory of non-radiation energy transfer. Changes in the CD and FT-IR spectra were observed upon ligand binding along with a significant degree of tryptophan fluorescence quenching on complex formation. Computational mapping of the possible binding sites of nobiletin revealed the molecule to be bound in the large hydrophobic cavity of subdomain IIA.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Luminescence - Volume 128, Issue 3, March 2008, Pages 513-520
Journal: Journal of Luminescence - Volume 128, Issue 3, March 2008, Pages 513-520
نویسندگان
Yuanyuan Yue, Yaheng Zhang, Ying Li, Jinhua Zhu, Jin Qin, Xingguo Chen,