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- Title
- An integrated study of tyrosinase inhibition by rutin: progress using a computational simulation = Rutin에 의한 타이로시네이즈 저해 통합 연구
- Author(s)
- Y X Si; S J Yin; Sang Ho Oh; Z J Wang; S Ye; J M Yang; Y D Park; Jinhyuk Lee; G Y Qian
- Bibliographic Citation
- Journal of Biomolecular Structure & Dynamics, vol. 29, no. 5, pp. 999-1012
- Publication Year
- 2012
- Abstract
- Tyrosinase inhibition studies have recently gained the attention of researchers due to their potential application values. We simulated docking (binding energies for AutoDock Vina: 29.1 kcal/mol) and performed a molecular dynamics simulation to verify docking results between tyrosinase and rutin. The docking results suggest that rutin mostly interacts with histidine residues located in the active site. A 10 ns molecular dynamics simulation showed that one copper ion at the tyrosinase active site was responsible for the interaction with rutin. Kinetic analyses showed that rutin-mediated inactivation followed a first-order reaction and mono- and biphasic rate constants occurred with rutin. The inhibition was a typical competitive type with Ki 5 1.10 6 0.25 mM. Measurements of intrinsic and ANS-binding fluorescences showed that rutin showed a relatively strong binding affinity for tyrosinase and one possible binding site that could be a copper was detected accompanying with a hydrophobic exposure of tyrosinase. Cell viability testing with rutin in HaCaT keratinocytes showed that no toxic effects were produced. Taken together, rutin has the potential to be a potent anti-pigment agent. The strategy of predicting tyrosinase inhibition based on hydroxyl group number and computational simulation may prove useful for the screening of potential tyrosinase inhibitors.
- Keyword
- Docking simulationHydroxyl groupInhibition kineticsTyrosinaseRutin
- ISSN
- 0739-1102
- Publisher
- T&F (Taylor & Francis)
- DOI
- http://dx.doi.org/10.1080/073911012010525028
- Type
- Article
- Appears in Collections:
- Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
- Files in This Item:
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