2022
DOI: 10.1002/jmr.2955
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Interaction mechanism of pelargonidin against tyrosinase by multi‐spectroscopy and molecular docking

Abstract: The interaction mechanism of pelargonidin (PG) with tyrosinase was investigated by multi-spectroscopy and molecular docking. As a result, PG had strong inhibitory activity on tyrosinase with the IC 50 value of 41.94 Â 10 À6 molÁL À1 . The inhibition type of PG against tyrosinase was determined as a mixed-mode. Meanwhile, the fluorescence of tyrosinase was quenched statically by PG, and accompanied by non-radiative energy transfer. The three-dimensional (3-D) fluorescence, ultravioletvisible spectroscopy (UV-Vi… Show more

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Cited by 4 publications
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“…S55 . The addition of compound 6f significantly reduced the absorption peak of TYR at 280 nm, indicating that compound 6f can significantly change the secondary structure of TYR, and the quenching mechanism was consistent with the results of fluorescence spectroscopy experiments ( Tao et al, 2022 ).…”
Section: Resultssupporting
confidence: 84%
“…S55 . The addition of compound 6f significantly reduced the absorption peak of TYR at 280 nm, indicating that compound 6f can significantly change the secondary structure of TYR, and the quenching mechanism was consistent with the results of fluorescence spectroscopy experiments ( Tao et al, 2022 ).…”
Section: Resultssupporting
confidence: 84%