Insight into the Inhibitory Activities of Diverse Ligands for Tyrosinase Using Ligand- and Structure-based Approaches

doi:10.11944/j.issn.1000-0518.2018.07.170332

Chinese Journal of Applied Chemistry ›› 2018, Vol. 35 ›› Issue (7): 788-794.DOI: 10.11944/j.issn.1000-0518.2018.07.170332

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Insight into the Inhibitory Activities of Diverse Ligands for Tyrosinase Using Ligand- and Structure-based Approaches

Haifeng TANG^a^b^c,Fengchao CUI^a^*(),Lunyang LIU^a^c,Yunqi LI^a^*()

^aKey Laboratory of Synthetic Rubber,Changchun Institute of Applied Chemistry,Chinese Academy of Sciences,Changchun 130022,China
^bSchool of Life Science,Jilin University,Changchun 130012,China
^cUniversity of Chinese Academy of Sciences,Beijing 100049,China.

Received:2017-09-12 Accepted:2018-01-10 Published:2018-07-06 Online:2018-07-06
Contact: Fengchao CUI,Yunqi LI
Supported by:
Supported by the National Natural Science Foundation of China(No.21374117, No.21504092), and the China Postdoctoral Science Foundation(No.2014M561310)

Abstract

Abstract:

The use of variant inhibitors to regulate the bioactivities of tyrosinase, which is the key enzyme in charge of the production of melanin and pigments, is a long-standing approach to design cosmetic and pharmaceutical products. The quantitative description of the structure-activity relationship of tyrosinase inhibitors is still unclear. In this study, we constructed descriptive models by integrating ligand- and structure-based approaches for such purpose. They provide correlation coefficients of 0.961 for implicit models and 0.775 for explicit model, respectively, to descript the activities of three tea polyphenols with the tyrosinase inhibitory activity order of (-)-Epicatechin gallate(ECG)>(-)-Epigallocatechin gallate(EGCG)>Gallic acid(G). As revealing from the descriptive models, entropy loss is more important than other features for determining inhibitory activity and thus the tyrosinase-ECG complex with the fewer conformational entropy loss has the strongest inhibitory activity in vitro among the four tea polyphenols. Moreover, residues including His57, His201, Asn202, His205 Glu192 and Val215 are the core of active sites in tyrosinase, and stabilize the tyrosinase-inhibitor complex by van der Waals and hydrogen bonding interactions.

Key words: tyrosinase, quantitative structure-activity relationship, molecular mechanics/Poisson Boltzmann surface area, Random Forest algorithm, Monte Carlo algorithm

Haifeng TANG,Fengchao CUI,Lunyang LIU,Yunqi LI. Insight into the Inhibitory Activities of Diverse Ligands for Tyrosinase Using Ligand- and Structure-based Approaches[J]. Chinese Journal of Applied Chemistry, 2018, 35(7): 788-794.

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Insight into the Inhibitory Activities of Diverse Ligands for Tyrosinase Using Ligand- and Structure-based Approaches

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