Issue 54, 2021

Inhibitory mechanism of two homoisoflavonoids from Ophiopogon japonicus on tyrosinase activity: insight from spectroscopic analysis and molecular docking

Abstract

The inhibition mechanism of two homoisoflavonoids from Ophiopogon japonicus including methylophiopogonanone A (MO-A) and methylophiopogonanone B (MO-B) on tyrosinase (Tyr) was studied by multiple spectroscopic techniques and molecular docking. The results showed that the two homoisoflavonoids both inhibited Tyr activity via a reversible mixed-inhibition, with a half inhibitory concentration (IC50) of (10.87 ± 0.25) × 10−5 and (18.76 ± 0.14) × 10−5 mol L−1, respectively. The fluorescence quenching and secondary structure change of Tyr caused by MO-A and B are mainly driven by hydrophobic interaction and hydrogen bonding. Molecular docking analysis indicated that phenylmalandioxin in MO-A and methoxy in MO-B could coordinate with a Cu ion in the active center of Tyr, and interacted with amino acid Glu322 to form hydrogen bonding, occupying the catalytic center to block the entry of the substrate and consequently inhibit Tyr activity. This study may provide new perspectives on the inhibition mechanism of MO-A and MO-B on Tyr and serve a scientific basis for screening effective Tyr inhibitors.

Graphical abstract: Inhibitory mechanism of two homoisoflavonoids from Ophiopogon japonicus on tyrosinase activity: insight from spectroscopic analysis and molecular docking

Article information

Article type
Paper
Submitted
12 Aug 2021
Accepted
08 Okt 2021
First published
22 Okt 2021
This article is Open Access
Creative Commons BY-NC license

RSC Adv., 2021,11, 34343-34354

Inhibitory mechanism of two homoisoflavonoids from Ophiopogon japonicus on tyrosinase activity: insight from spectroscopic analysis and molecular docking

L. Wang, Y. Qin, Y. Wang, Y. Zhou, B. Liu, M. Bai, X. Tong, R. Fang and X. Huang, RSC Adv., 2021, 11, 34343 DOI: 10.1039/D1RA06091K

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