کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1987737 1540310 2008 9 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Interaction of bovine serum albumin with some novel PEG-containing diblock copolymers
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Interaction of bovine serum albumin with some novel PEG-containing diblock copolymers
چکیده انگلیسی

A comparative study on the interaction of different PEG-containing diblock copolymers including SA400, SA600, SA1500 and OA1500 (stearyl and oleyl esters of polyethylene glycol with 400, 600 and 1500 molecular weights, respectively) with bovine serum albumin (BSA) was carried out using isothermal titration calorimetry (ITC), attenuated total reflectance Fourier transform infrared (ATR-FTIR), circular dichroism (CD), and fluorescence spectroscopies. ITC data show that SA400, SA600, SA1500 and OA1500 bind to BSA, with association constants of (14.5, 3.16, 50.7 and 17.6) × 103 M−1, respectively. Results also show that the binding is enthalpically driven, disfavored by conformational entropy. Quantitative analysis of the FTIR absorbance spectra at amide I′ (1600–1700 cm−1) as well as far UV circular dichroism data show that these polymers do not disturb the BSA structure and only cause a slight increment in helicity along with a slight decrease in the β-structure. Only stearyl esters SA400 and SA1500 slightly decreased the random structure content of the BSA. The diblock copolymers inhibit protein aggregation and bind to BSA better than their constituent PEGs causing an increment in its Tm; SA1500 is showing the strongest effect.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 43, Issue 3, 1 October 2008, Pages 262–270
نویسندگان
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