2-(4-Fluorophenyl)-quinazolin-4(3H)-one as a novel tyrosinase inhibitor: Synthesis,inhibitory activity,and mechanism |
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| Institution: | 1. Key Laboratory of Small Fuctional Organic Molecule, Ministry of Education and College of Life Science, Jiangxi Normal University, Nanchang, Jiangxi 330022, China;2. Key Laboratory of Green Chemistry, Nanchang, Jiangxi 330022, China;1. Research Institute of Pharmaceutical Sciences, College of Pharmacy, Kyungpook National University, 80 Daehak-ro, Buk-gu, Daegu 702-701, Republic of Korea;2. College of Pharmacy, Gachon University, Incheon 406-799, Republic of Korea;1. Department of Biology, College of Natural Sciences, Kongju National University, Gongju 314-701, Republic of Korea;2. Department of Chemistry, Allama Iqbal Open University, Islamabad 44000, Pakistan;3. Atta-ur-Rahman School of Applied Biosciences, National University of Sciences and Technology, H-12, Kashmir Highway, Islamabad 44000, Pakistan;1. Key Laboratory of Small Fuctional Organic Molecule, Ministry of Education and College of Life Science, Jiangxi Normal University, Nanchang, Jiangxi 330022, China;2. Key Laboratory of Green Chemistry, Jiangxi Province, Nanchang, Jiangxi 330022, China;1. Key Laboratory of Medicinal Chemistry for Natural Resource (Yunnan University), Ministry Education, School of Chemical Science and Technology, Yunnan University, Kunming 650091, PR China;2. Institute of Microbiology, Yunnan University, Kunming 650091, PR China;3. Yunnan Tumor Research Institute, The Third Affiliated Hospital of Kunming Medical University, Kunming 650118, PR China;1. State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, PR China;2. Department of Chemistry, Nanchang University, Nanchang 330031, PR China |
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| Abstract: | 2-(4-Fluorophenyl)-quinazolin-4(3H)-one (FQ) was synthesized, and its structure was identified with 1H nuclear magnetic resonance (1H NMR), 13C nuclear magnetic resonance (13C NMR), fourier transform infrared spectroscopy (FTIR), and high resolution mass spectrometry (HRMS). From the enzyme analysis, the results showed that it could inhibit the diphenolase activity of tyrosinase (IC50 = 120 ± 2 μM). Furthermore, the results of kinetic studies showed that the compound was a reversible mixed-type inhibitor, and that the inhibition constants were determined to be 703.2 (KI) and 222.1 μM (KIS). The results of fluorescence quenching experiment showed that the compound could interact with tyrosinase and the substrates (tyrosine and l-DOPA). Molecular docking analysis revealed that the mass transfer rate was affected by FQ blocking the enzyme catalytic center. In brief, current study identified a novel tyrosinase inhibitor which deserved further study for hyperpigmentation drugs. |
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| Keywords: | Quinazolinone Synthesis Tyrosinase inhibitor Fluorescence Molecular docking |
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