Unknown

Dataset Information

0

Tyrosinase Inhibition and Kinetic Details of Puerol A Having But-2-Enolide Structure from Amorpha fruticosa.


ABSTRACT: Puerol A (1) from Amorpha fruticosa showed highly potent inhibition against both monophenolase (IC50 = 2.2 ?M) and diphenolase (IC50 = 3.8 ?M) of tyrosinase. We tried to obtain a full story of enzyme inhibitory behavior for inhibitor 1 because the butenolide skeleton has never been reported as a tyrosinase inhibitor. Puerol A was proved as a reversible, competitive, simple slow-binding inhibitor, according to the respective parameters; k3 = 0.0279 ?M-1 min-1 and k4 = 0.003 min-1. A longer lag-phase and a reduced static-state activity of the enzyme explained that puerol A had a tight formation of the complex with Emet. Dose-dependent inhibition was also confirmed by high-performance liquid chromatography (HPLC) analysis using N-acetyl-l-tyrosine as a substrate, which was completely inhibited at 20 ?M. A high binding affinity of 1 to tyrosinase was confirmed by fluorescence quenching analysis. Moreover, puerol A decreased melanin content in the B16 melanoma cell dose-dependently with an IC50 of 11.4 ?M.

SUBMITTER: Kim JH 

PROVIDER: S-EPMC7287670 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

Tyrosinase Inhibition and Kinetic Details of Puerol A Having But-2-Enolide Structure from <i>Amorpha fruticosa</i>.

Kim Jeong Ho JH   Jang Da Hyun DH   Lee Ki Won KW   Kim Kwang Dong KD   Shah Abdul Bari AB   Zhumanova Kamila K   Park Ki Hun KH  

Molecules (Basel, Switzerland) 20200518 10


Puerol A (<b>1</b>) from <i>Amorpha fruticosa</i> showed highly potent inhibition against both monophenolase (IC<sub>50</sub> = 2.2 μM) and diphenolase (IC<sub>50</sub> = 3.8 μM) of tyrosinase. We tried to obtain a full story of enzyme inhibitory behavior for inhibitor <b>1</b> because the butenolide skeleton has never been reported as a tyrosinase inhibitor. Puerol A was proved as a reversible, competitive, simple slow-binding inhibitor, according to the respective parameters; <i>k</i><sub>3</s  ...[more]

Similar Datasets

| S-EPMC4674871 | biostudies-other
| S-EPMC7664916 | biostudies-literature
| S-EPMC7181007 | biostudies-literature
| PRJNA319365 | ENA
| S-EPMC8471001 | biostudies-literature
| S-EPMC6272459 | biostudies-literature
| S-EPMC7993013 | biostudies-literature
| S-EPMC7183614 | biostudies-literature
| S-EPMC5564602 | biostudies-other
| S-EPMC5685642 | biostudies-literature