AI Article Synopsis
- Inhibition of mushroom tyrosinase was effectively achieved using synthetic dihydropyrano[3,2-b]chromenediones, particularly DHPC04, which showed strong activity comparable to the standard inhibitor kojic acid.
- Kinetic studies indicated that these compounds act as competitive inhibitors at the L-DOPA binding site of the enzyme.
- Molecular modeling further revealed key insights into how these compounds interact with the copper active site of tyrosinase.
Article Abstract
Inhibition of mushroom tyrosinase was observed with synthetic dihydropyrano[3,2-b]chromenediones. Among them, DHPC04 displayed the most potent tyrosinase inhibitory activity with a K value of 4 μm, comparable to the reference standard inhibitor kojic acid. A kinetic study suggested that these synthetic heterocyclic compounds behave as competitive inhibitors for the L-DOPA binding site of the enzyme. Furthermore, molecular modeling provided important insight into the mechanism of binding interactions with the tyrosinase copper active site.
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| http://dx.doi.org/10.1111/cbdd.13001 | DOI Listing |
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