کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
8334926 1540275 2012 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Kinetic, structural and molecular docking studies on the inhibition of tyrosinase induced by arabinose
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Kinetic, structural and molecular docking studies on the inhibition of tyrosinase induced by arabinose
چکیده انگلیسی
Tyrosinase plays a central role in biological pigment formation, and hence knowledge of tyrosinase catalytic mechanisms and regulation may have medical, cosmetic, and agricultural applications. We found in this study that arabinose significantly inhibited tyrosinase, and this was accompanied by conformational changes in enzyme structure. Kinetic analysis showed that arabinose-mediated inactivation followed first-order kinetics, and single and multiple classes of rate constants were measured. Arabinose displayed a mixed-type inhibitory mechanism with Ki = 0.22 ± 0.07 mM. Measurements of intrinsic and ANS-binding fluorescence showed that arabinose induced tyrosinase to unfold and expose inner hydrophobic regions. We simulated the docking between tyrosinase and arabinose (binding energies were −26.28 kcal/mol for Dock6.3 and −2.02 kcal/mol for AutoDock4.2) and results suggested that arabinose interacts mostly with His61, Asn260, and Met280. The present strategy of predicting tyrosinase inhibition by simulation of docking by hydroxyl groups may prove useful in screening for potential tyrosinase inhibitors, as shown here for arabinose.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 50, Issue 3, 1 April 2012, Pages 694-700
نویسندگان
, , , , , , , ,