کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
4754363 1418060 2017 21 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Photochemistry and mechanism of designed pyrenyl probe towards promoted cleavage of proteins
ترجمه فارسی عنوان
فتوشیمی و مکانیسم پروب پریانیل طراحی شده به سمت تکه شدن پروتئین ها
کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه مهندسی شیمی بیو مهندسی (مهندسی زیستی)
چکیده انگلیسی
A new photochemical reagent, succinic acid-1(1-pyrene)methylamide (PMA-SUC), was developed to recognize the specific binding sites on model proteins, egg-white lysozyme and avidin. The interaction of the photochemical reagent with the proteins was studied by UV-Vis, fluorescence spectroscopic methods and docking description. PMA-SUC was found to bind to lysozyme and avidin with binding constants (Kb) of 2.4 × 105 and 6.7 × 105 (M− 1), respectively. The fluorescence intensity of PMA-SUC decreased with increasing concentration of both proteins. Quenching of PMA-SUC fluorescence, in the absence and presence of the protein by an electron acceptor (Hexaamminecobalt(III) chloride, Co(NH3)6Cl3) showed no significant changes in the Ksv values (Stern-Volmer quenching constant), indicating that PMA-SUC bound to the hydrophilic sites or near the surface of the proteins. Irradiation of protein-PMA-SUC mixture, at 342 nm for a period of time, in the presence of Co(NH3)6Cl3 as an electron acceptor, resulted in the cleavage of both proteins with high specificity. Binding mechanisms were studied using Molecular docking method. Molecular docking study indicated the position of PMA-SUC upon binding to the proteins by hydrogen bonding interaction with donor-acceptor within the distance of less than 5 Å in the minimum of binding free energy. The docking results have supported the results obtained from the spectroscopic methods and cleavage studies.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 173, August 2017, Pages 35-42
نویسندگان
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