Anilino-1,4-naphthoquinones as potent mushroom tyrosinase inhibitors: in vitro and in silico studies
Tyrosinase, a pivotal enzyme in melanin synthesis, is a primary target for the development of depigmenting agents. In this work, in vitro and in silico techniques were employed to identify novel tyrosinase inhibitors from a set of 12 anilino-1,4-naphthoquinone derivatives. Results from the mushroom...
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| Format: | Article |
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Taylor & Francis Group
2024-12-01
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| Series: | Journal of Enzyme Inhibition and Medicinal Chemistry |
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| Online Access: | https://www.tandfonline.com/doi/10.1080/14756366.2024.2357174 |
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| author | Sahachai Sabuakham Sutita Nasoontorn Napat Kongtaworn Thanyada Rungrotmongkol Atit Silsirivanit Ratchanok Pingaew Panupong Mahalapbutr |
| author_facet | Sahachai Sabuakham Sutita Nasoontorn Napat Kongtaworn Thanyada Rungrotmongkol Atit Silsirivanit Ratchanok Pingaew Panupong Mahalapbutr |
| author_sort | Sahachai Sabuakham |
| collection | DOAJ |
| description | Tyrosinase, a pivotal enzyme in melanin synthesis, is a primary target for the development of depigmenting agents. In this work, in vitro and in silico techniques were employed to identify novel tyrosinase inhibitors from a set of 12 anilino-1,4-naphthoquinone derivatives. Results from the mushroom tyrosinase activity assay indicated that, among the 12 derivatives, three compounds (1, 5, and 10) demonstrated the most significant inhibitory activity against mushroom tyrosinase, surpassing the effectiveness of the kojic acid. Molecular docking revealed that all studied derivatives interacted with copper ions and amino acid residues at the enzyme active site. Molecular dynamics simulations provided insights into the stability of enzyme–inhibitor complexes, in which compounds 1, 5, and particularly 10 displayed greater stability, atomic contacts, and structural compactness than kojic acid. Drug likeness prediction further strengthens the potential of anilino-1,4-naphthoquinones as promising candidates for the development of novel tyrosinase inhibitors for the treatment of hyperpigmentation disorders. |
| format | Article |
| id | doaj-art-d0ec918f5481445ba291035eee6d50d2 |
| institution | DOAJ |
| issn | 1475-6366 1475-6374 |
| language | English |
| publishDate | 2024-12-01 |
| publisher | Taylor & Francis Group |
| record_format | Article |
| series | Journal of Enzyme Inhibition and Medicinal Chemistry |
| spelling | doaj-art-d0ec918f5481445ba291035eee6d50d22025-08-20T02:40:33ZengTaylor & Francis GroupJournal of Enzyme Inhibition and Medicinal Chemistry1475-63661475-63742024-12-0139110.1080/14756366.2024.2357174Anilino-1,4-naphthoquinones as potent mushroom tyrosinase inhibitors: in vitro and in silico studiesSahachai Sabuakham0Sutita Nasoontorn1Napat Kongtaworn2Thanyada Rungrotmongkol3Atit Silsirivanit4Ratchanok Pingaew5Panupong Mahalapbutr6Department of Biochemistry, Center for Translational Medicine, Faculty of Medicine, Khon Kaen University, Khon Kaen, ThailandDepartment of Biochemistry, Center for Translational Medicine, Faculty of Medicine, Khon Kaen University, Khon Kaen, ThailandProgram in Bioinformatics and Computational Biology, Graduate School, Chulalongkorn University, Bangkok, ThailandProgram in Bioinformatics and Computational Biology, Graduate School, Chulalongkorn University, Bangkok, ThailandDepartment of Biochemistry, Center for Translational Medicine, Faculty of Medicine, Khon Kaen University, Khon Kaen, ThailandDepartment of Chemistry, Faculty of Science, Srinakharinwirot University, Bangkok, ThailandDepartment of Biochemistry, Center for Translational Medicine, Faculty of Medicine, Khon Kaen University, Khon Kaen, ThailandTyrosinase, a pivotal enzyme in melanin synthesis, is a primary target for the development of depigmenting agents. In this work, in vitro and in silico techniques were employed to identify novel tyrosinase inhibitors from a set of 12 anilino-1,4-naphthoquinone derivatives. Results from the mushroom tyrosinase activity assay indicated that, among the 12 derivatives, three compounds (1, 5, and 10) demonstrated the most significant inhibitory activity against mushroom tyrosinase, surpassing the effectiveness of the kojic acid. Molecular docking revealed that all studied derivatives interacted with copper ions and amino acid residues at the enzyme active site. Molecular dynamics simulations provided insights into the stability of enzyme–inhibitor complexes, in which compounds 1, 5, and particularly 10 displayed greater stability, atomic contacts, and structural compactness than kojic acid. Drug likeness prediction further strengthens the potential of anilino-1,4-naphthoquinones as promising candidates for the development of novel tyrosinase inhibitors for the treatment of hyperpigmentation disorders.https://www.tandfonline.com/doi/10.1080/14756366.2024.2357174Tyrosinase inhibitionanilino-14-naphthoquinonesmolecular dockingmolecular dynamics simulations |
| spellingShingle | Sahachai Sabuakham Sutita Nasoontorn Napat Kongtaworn Thanyada Rungrotmongkol Atit Silsirivanit Ratchanok Pingaew Panupong Mahalapbutr Anilino-1,4-naphthoquinones as potent mushroom tyrosinase inhibitors: in vitro and in silico studies Journal of Enzyme Inhibition and Medicinal Chemistry Tyrosinase inhibition anilino-14-naphthoquinones molecular docking molecular dynamics simulations |
| title | Anilino-1,4-naphthoquinones as potent mushroom tyrosinase inhibitors: in vitro and in silico studies |
| title_full | Anilino-1,4-naphthoquinones as potent mushroom tyrosinase inhibitors: in vitro and in silico studies |
| title_fullStr | Anilino-1,4-naphthoquinones as potent mushroom tyrosinase inhibitors: in vitro and in silico studies |
| title_full_unstemmed | Anilino-1,4-naphthoquinones as potent mushroom tyrosinase inhibitors: in vitro and in silico studies |
| title_short | Anilino-1,4-naphthoquinones as potent mushroom tyrosinase inhibitors: in vitro and in silico studies |
| title_sort | anilino 1 4 naphthoquinones as potent mushroom tyrosinase inhibitors in vitro and in silico studies |
| topic | Tyrosinase inhibition anilino-14-naphthoquinones molecular docking molecular dynamics simulations |
| url | https://www.tandfonline.com/doi/10.1080/14756366.2024.2357174 |
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