An ultrafiltration high-performance liquid chromatography coupled with diode array detector and mass spectrometry approach for screening and characterising tyrosinase inhibitors from mulberry leaves

Analytica Chimica Acta
Zhenzhong YangYiyu Cheng

Abstract

Tyrosinase is a key enzyme in melanin synthesis. Its inhibitor may be used to efficiently treat hyperpigmentation and widely applied in cosmetic products and food supplements. In the present study, a new assay based on ultrafiltration high-performance liquid chromatography coupled with diode array detector and mass spectrometry (HPLC-DAD-MS) was developed for the rapid screening and identification of ligands for tyrosinase. Experiments were carried out to select the optimal binding conditions, tyrosinase concentration, and incubation time. Non-specific binding to the denatured tyrosinase was also investigated. Twelve compounds with tyrosinase binding activity were found in mulberry leaf extracts. The identities of these compounds were characterised by HPLC-DAD-MS(n). Particularly, two compounds, namely, quercetin-3-O-(6-O-malonyl)-β-D-glucopyranoside and kaempferol-3-O-(6-O-malonyl)-β-D-glucopyranoside, were identified as new tyrosinase inhibitors. The screening results were verified by tyrosinase inhibition assays. Experimental results proved that the proposed method could rapidly screen tyrosinase inhibitors in complex mixtures.

References

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Citations

Jul 9, 2013·Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences·Liangliang LiuMijun Peng
Dec 10, 2013·Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences·Karina Bora de OliveiraBrás Heleno de Oliveira
Sep 27, 2016·Journal of Pharmaceutical and Biomedical Analysis·Han WeiGuanghua Wu
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Jul 1, 2017·BioMed Research International·Yung-Sheng LinWen-Ying Huang
Feb 9, 2019·Journal of Enzyme Inhibition and Medicinal Chemistry·Samaneh ZolghadriAli Akbar Saboury
Jan 9, 2021·Signal Transduction and Targeted Therapy·Dehua YangMing-Wei Wang
Sep 29, 2021·Journal of Enzyme Inhibition and Medicinal Chemistry·Xiao-Wei ZhangDe-Qiang Li

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