کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10533811 | 961894 | 2005 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Equilibrium studies of a fluorescent tacrolimus binding to surfactant protein A
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موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Tacrolimus (FK506) is a hydrophobic immunosuppressive agent used in kidney, liver, and lung transplantation. The objective of this study was to characterize the binding of FK506 to surfactant protein A (SP-A), an abundant lipoprotein found in the alveolar fluid that functions as part of the innate immune system in the lung. We have synthesized a novel derivative of FK506 in which a dansyl moiety was covalently bound via cadaverine to the C22 position of the FK506 molecule (DNS-FK). Using the fluorescence and anisotropy properties of DNS-FK, we demonstrated that tacrolimus avidly binds to SP-A with an apparent equilibrium association constant (Kapp) of 107Â Mâ1 and a Gibbs binding free energy of â40Â kJÂ molâ1Â Kâ1. Derivatization of FK506 at the C22 position did not block FK506 binding to the cytosolic immunophilin FK506-binding protein (FK-BP) or human serum albumin (HSA), both used as controls of tacrolimus-binding proteins. Kapp for FK-BP/DNS-FK and HSA/DNS-FK complexes were 1.5Â ÃÂ 107 and 107Â Mâ1, respectively. The high sensitivity of this analytical technique makes it suitable for binding analysis of FK506 to proteins.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Analytical Biochemistry - Volume 340, Issue 1, 1 May 2005, Pages 57-65
Journal: Analytical Biochemistry - Volume 340, Issue 1, 1 May 2005, Pages 57-65
نویسندگان
Olga Cañadas, Alejandra Sáenz, Guillermo Orellana, Cristina Casals,