Effects of Isorhamnetin on Tyrosinase: Inhibition Kinetics and Computational Simulation
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- SI Yue-Xiu
- College of Biological and Environmental Sciences, Zhejiang Wanli University
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- WANG Zhi-Jiang
- College of Biological and Environmental Sciences, Zhejiang Wanli University
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- PARK Daeui
- Molecular Inflammation Research Center for Aging Intervention (MRCA), College of Pharmacy, Pusan National University
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- JEONG Hyoung Oh
- Molecular Inflammation Research Center for Aging Intervention (MRCA), College of Pharmacy, Pusan National University
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- YE Sen
- College of Biological and Environmental Sciences, Zhejiang Wanli University
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- CHUNG Hae Young
- Molecular Inflammation Research Center for Aging Intervention (MRCA), College of Pharmacy, Pusan National University
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- YANG Jun-Mo
- Department of Dermatology, Sungkyunkwan University School of Medicine, Samsung Medical Center
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- YIN Shang-Jun
- College of Biological and Environmental Sciences, Zhejiang Wanli University
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- QIAN Guo-Ying
- College of Biological and Environmental Sciences, Zhejiang Wanli University
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Abstract
We studied the inhibitory effects of isorhamnetin on mushroom tyrosinase by inhibition kinetics and computational simulation. Isorhamnetin reversibly inhibited tyrosinase in a mixed-type manner at Ki=0.235 ± 0.013 mM. Measurements of intrinsic and 1-anilinonaphthalene-8-sulfonate(ANS)-binding fluorescence showed that isorhamnetin did not induce significant changes in the tertiary structure of tyrosinase. To gain insight into the inactivation process, the kinetics were computed via time-interval measurements and continuous substrate reactions. The results indicated that inactivation induced by isorhamnetin was a first-order reaction with biphasic processes. To gain further insight, we simulated docking between tyrosinase and isorhamnetin. Simulation was successful (binding energies for Dock6.3: −32.58 kcal/mol, for AutoDock4.2: −5.66 kcal/mol, and for Fred2.2: −48.86 kcal/mol), suggesting that isorhamnetin interacts with several residues, such as HIS244 and MET280. This strategy of predicting tyrosinase interaction in combination with kinetics based on a flavanone compound might prove useful in screening for potential natural tyrosinase inhibitors.
Journal
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 76 (6), 1091-1097, 2012
Japan Society for Bioscience, Biotechnology, and Agrochemistry
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Details 詳細情報について
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- CRID
- 1390282681454684416
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- NII Article ID
- 10030817793
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- NII Book ID
- AA10824164
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- COI
- 1:STN:280:DC%2BC38jps1GitQ%3D%3D
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- ISSN
- 13476947
- 09168451
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- NDL BIB ID
- 023768100
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- PubMed
- 22790928
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- Abstract License Flag
- Disallowed