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- W4229077051 abstract "The interactions between pelargonidin with tyrosinase have been investigated. Through the pelargonidin structure figure, inhibition rate figure, fluorescence quenching figure and molecular docking figure composition of the graphical abstract. Results revealed that pelargonidin caused the fluorescence static quenching of tyrosinase protein. Van der Waals force or Hydrogen bonding force play major role in the binding process and the inhibition type of PG against tyrosinase was determined as a mixed mode." @default.
- W4229077051 created "2022-05-08" @default.
- W4229077051 date "2022-06-01" @default.
- W4229077051 modified "2023-09-23" @default.
- W4229077051 doi "https://doi.org/10.1002/jmr.v35.6" @default.
- W4229077051 hasPublicationYear "2022" @default.
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