Integration of molecular docking and molecular dynamics simulations for studying potential tyrosinase inhibitors from sargassum genus

Thi Minh Tuyet Dang; Thanh Vinh Nguyen; Duy Phong Tran; Minh Quan Pham; Hai Dang Nguyen; Thi Nguyet Hang Nguyen; Nguyen Thanh Long Bui; Ngoc Hung Truong; Pham Quoc Long

doi:10.15625/2525-2518/22658

Author affiliations

Authors

Thi Minh Tuyet Dang Institute of Natural Products Chemistry, Vietnam Academy of Science and Technology, 18 Hoang Quoc Viet, Cau Giay, Ha Noi, Viet Nam https://orcid.org/0009-0002-9880-0323
Thanh Vinh Nguyen Faculty of Pharmacy, University of Pécs https://orcid.org/0009-0007-5864-6866
Duy Phong Tran Vietnam Institute of Science Technology and Innovation, Ministry of Science and Technology https://orcid.org/0009-0001-0555-8949
Minh Quan Pham Institute of Natural Products Chemistry, Vietnam Academy of Science and Technology https://orcid.org/0000-0001-6922-1627
Hai Dang Nguyen Institute of Natural Products Chemistry, Vietnam Academy of Science and Technology https://orcid.org/0009-0004-7128-2065
Thi Nguyet Hang Nguyen Institute of Natural Products Chemistry, Vietnam Academy of Science and Technology
Nguyen Thanh Long Bui https://orcid.org/0009-0001-6033-6038
Ngoc Hung Truong Laboratory of Biophysics, Institute for Advanced Study in Technology, Ton Duc Thang University https://orcid.org/0000-0001-7904-1785
Pham Quoc Long Institute of Natural Products Chemistry, Vietnam Academy of Science and Technology / Section Editor of Vietnam Journal of Science and Technology

DOI:

https://doi.org/10.15625/2525-2518/22658

Keywords:

molecular docking, molecular dynamics, sargassum, tyrosinase inhibtors

Abstract

The copper-dependent enzyme tyrosinase is vital for the creation of melanin, the pigment responsible for coloration in skin, hair, and eyes. Because of tyrosinase's contribution to unwanted skin darkening, the identification of secure and potent natural inhibitors is a major goal for scientists in the cosmetic and pharmaceutical industries. In this work, a dataset of 71 compounds originated from Sargassum genus has been investigated the ligand-binding affinity to tyrosinase via atomistic simulations. The compounds including difucodiphlorethol A and pseudotrifuhalol A were suggested that can inhibit GSK-3β via molecular docking and molecular dynamic simulations. The residues including His61, His259, Asn260, His263, Arg268, Met280, Gly281, Ser282 and Val283 play a crucial role in the ligand-binding process Furthermore, the toxicity prediction also indicates that these compounds would adopt less toxicity.

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