Evidence map›Paper›PMID 35542029›Full record

ArticleRSC advances2018

Understanding the inhibitory mechanism of tea polyphenols against tyrosinase using fluorescence spectroscopy, cyclic voltammetry, oximetry, and molecular simulations.

Haifeng Tang, Fengchao Cui, Haijuan Li, Qingrong Huang, Yunqi Li

Open access · goldAbstract read
In one paragraph

Article in RSC advances, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.9field-weighted citation impact, top 16% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Antioxidants (Basel, Switzerland) · 2026
    Article
  3. Integrated LC-HRMS and HPLC Profiling of Fourteen AnatolianPharmaceuticals (Basel, Switzerland) · 2026
    Article
  4. Article
  5. Article
  6. Anilino-1,4-naphthoquinones as potent mushroom tyrosinase inhibitors:Journal of enzyme inhibition and medicinal chemistry · 2024
    Article
  7. Article
  8. A potentiometric and spectrofluorimetric approach to unravel inhibitory effects of semi- and thiosemicarbazones on mushroom tyrosinase activity.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2023
    Article
  9. Article
  10. Review
  11. Article
  12. Plants (Basel, Switzerland) · 2021
    Review
  13. Review
  14. A comprehensive review on tyrosinase inhibitors.Journal of enzyme inhibition and medicinal chemistry · 2019
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 3 countries.

Haifeng TangKey Laboratory of Synthetic Rubber, Changchun Institute of Applied Chemistry (CIAC), Chinese Academy of Sciences Changchun Jilin 130022 P. R. China fccui@ciac.ac.cn yunqi@ciac.ac.cn.
Fengchao CuiKey Laboratory of Synthetic Rubber, Changchun Institute of Applied Chemistry (CIAC), Chinese Academy of Sciences Changchun Jilin 130022 P. R. China fccui@ciac.ac.cn yunqi@ciac.ac.cn.ORCID https://orcid.org/0000-0002-1985-1994
Haijuan LiState Key Laboratory of Electroanalytical Chemistry, Changchun Institute of Applied Chemistry (CIAC), Chinese Academy of Sciences Changchun Jilin 130022 P. R. China.
Qingrong HuangDepartment of Food Science, Rutgers University 65 Dudley Road New Brunswick NJ 08901 USA.ORCID https://orcid.org/0000-0002-6103-9000
Yunqi LiKey Laboratory of Synthetic Rubber, Changchun Institute of Applied Chemistry (CIAC), Chinese Academy of Sciences Changchun Jilin 130022 P. R. China fccui@ciac.ac.cn yunqi@ciac.ac.cn.ORCID https://orcid.org/0000-0002-5190-3037
Chinese Academy of Sciences · CNJilin University · CNRutgers, The State University of New Jersey · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Inhibiting the activity of tyrosinase is a very effective and safe way to prevent enzymatic browning in food and to resist pests in agriculture. Tea polyphenols (TPs), regarded as safe and non-toxic food additives, have been reported due to their potential inhibitory capability against tyrosinase, but their ambiguous inhibitory mechanisms have severely limited their application. In the present work, fluorescence spectroscopy, cyclic voltammetry (CV), oximetry and molecular simulation approaches were employed to shed light on the underlying inhibitory mechanisms of TPs with different structures including (+)-catechin, (-)-epicatechin gallate (ECG) and (-)-epigallocatechin gallate (EGCG) against tyrosinase. Fluorescence spectra show that the three TPs are capable of binding tyrosinase with a molar proportion of 1 : 1. The analysis of CV curves and oxygen utilization suggests that these three TPs can be oxidized by tyrosinase, revealing that these three TPs are suicide inhibitors of tyrosinase. Furthermore, ECG and catechin make tyrosinase irreversibly inactivated due to their catechol group (ring B) being catalyzed by tyrosinase through a cresolase-like pathway, while EGCG inhibits the activity of tyrosinase by competing with or delaying the oxidation of substrate. Molecular simulations further confirm that ring B of ECG and catechin makes a significant contribution to tyrosinase inhibitory activities, and has a direct interaction with the coupled binuclear copper ions in the optimal orientation required by the cresolase-like pathway.

Identifiers

PMID35542029
PMCPMC9078569
OpenAlexW2788715888

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.