Effects of Isorhamnetin on Tyrosinase: Inhibition Kinetics and Computational Simulation

DOI Web Site PubMed 参考文献58件
  • SI Yue-Xiu
    College of Biological and Environmental Sciences, Zhejiang Wanli University
  • WANG Zhi-Jiang
    College of Biological and Environmental Sciences, Zhejiang Wanli University
  • PARK Daeui
    Molecular Inflammation Research Center for Aging Intervention (MRCA), College of Pharmacy, Pusan National University
  • JEONG Hyoung Oh
    Molecular Inflammation Research Center for Aging Intervention (MRCA), College of Pharmacy, Pusan National University
  • YE Sen
    College of Biological and Environmental Sciences, Zhejiang Wanli University
  • CHUNG Hae Young
    Molecular Inflammation Research Center for Aging Intervention (MRCA), College of Pharmacy, Pusan National University
  • YANG Jun-Mo
    Department of Dermatology, Sungkyunkwan University School of Medicine, Samsung Medical Center
  • YIN Shang-Jun
    College of Biological and Environmental Sciences, Zhejiang Wanli University
  • QIAN Guo-Ying
    College of Biological and Environmental Sciences, Zhejiang Wanli University

この論文をさがす

抄録

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.

収録刊行物

参考文献 (58)*注記

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ