Tyrosinase and α-glucosidase inhibitory potential of compounds isolated from Quercus coccifera bark: In vitro and in silico perspectives |
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| Institution: | 1. Hacettepe University, Faculty of Pharmacy, Department of Pharmaceutical Chemistry, S?hhiye, Ankara, TR-06100 Ankara, Turkey;2. Karadeniz Technical University, Faculty of Pharmacy, Department of Biochemistry, Trabzon, Turkey;3. Karadeniz Technical University, Drug and Pharmaceutical Technology Application and Research Center, Trabzon, Turkey;4. Hacettepe University, Faculty of Pharmacy, Department of Pharmacognosy, S?hhiye, Ankara, TR-06100 Ankara, Turkey;1. CAS Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences, Qingdao, 266071, China;2. Laboratory for Marine Drugs and Bioproducts, Qingdao National Laboratory for Marine Science and Technology, Qingdao, 266237, China;3. University of Chinese Academy of Sciences, Beijing, 100049, China;4. College of Marine Life Science, Ocean University of China, Qingdao, 266100, China;1. Modern Research Center for Traditional Chinese Medicine, Beijing University of Chinese Medicine, Beijing 100029, People''s Republic of China;2. School of Chinese Materia Medica, Beijing University of Chinese Medicine, Beijing 100102, People''s Republic of China;1. Chulabhorn Research Institute, Kamphaeng Phet 6, Talat Bang Khen, Lak Si, Bangkok 10210, Thailand;2. Faculty of Pharmaceutical Sciences, Khon Kaen University, Khon Kaen 40002, Thailand;1. School of Chinese Materia Medica, Tianjin University of Traditional Chinese Medicine, Tianjin 300193, PR China;2. Tianjin State Key Laboratory of Modern Chinese Medicine, Tianjin University of Traditional Chinese Medicine, Tianjin 300193, PR China;3. College of Science and Technology, Agricultural University of Hebei, Cangzhou 061100, PR China;1. Institute of Pharmacy/Pharmacognosy and Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck, 6020, Innsbruck, Austria;2. MCI Management Center Innsbruck, Maximilianstraße 2, 6020, Innsbruck, Austria;3. Institute of Pharmacy/Pharmaceutical Chemistry and Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck, 6020, Innsbruck, Austria;4. Cura Marketing GmbH, Doktor-Franz-Werner Straße 19, 6020, Innsbruck, Austria;5. Skin Research Institute, Cura Marketing GmbH, Doktor-Franz-Werner-Straße 19, 6020, Innsbruck, Austria;6. Institute of Botany, University of Innsbruck, Sternwartestraße15, 6020, Innsbruck, Austria;1. Hacettepe University, Faculty of Pharmacy, Department of Pharmaceutical Chemistry, S?hhiye, Ankara, TR-06100 Ankara, Turkey;2. Karadeniz Technical University, Faculty of Pharmacy, Department of Biochemistry, Trabzon, Turkey;3. Karadeniz Technical University, Drug and Pharmaceutical Technology Application and Research Center, Trabzon, Turkey;4. Hacettepe University, Faculty of Pharmacy, Department of Pharmacognosy, S?hhiye, Ankara, Turkey |
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| Abstract: | Bark of Quercus coccifera is widely used in folk medicine. We tested tyrosinase and α-glucosidase inhibitory effects of Q. coccifera bark extract and isolated compounds from it. The extract inhibited tyrosinase with an IC50 value of 75.13 ± 0.44 µg/mL. Among the isolated compounds, polydatin (6) showed potent tyrosinase inhibition compared to the positive control, kojic acid, with an IC50 value of 4.05 ± 0.30 µg/mL. The Q. coccifera extract also inhibited α-glucosidase significantly with an IC50 value of 3.26 ± 0.08 µg/mL. (-)-8-Chlorocatechin (5) was the most potent isolate, also more potent than the positive control, acarbose, with an IC50 value of 43.60 ± 0.67 µg/mL. According to the kinetic analysis, 6 was a noncompetitive and 5 was a competitive inhibitor of tyrosinase, and 5 was a noncompetitive α-glucosidase inhibitor. In the light of these findings, we performed in silico molecular docking studies for 5 and 6 with QM/MM optimizations to predict their tyrosinase inhibition mechanisms at molecular level and search for correlations with the in vitro results. We found that the ionized form of 5 (5i) showed higher affinity and more stable binding to tyrosinase catalytic site than its neutral form, while 6 bound to the predicted allosteric sites of the enzyme better than the catalytic site. |
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| Keywords: | α-Glucosidase Tyrosinase Polydatin Molecular modelling |
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