دورية أكاديمية
Potent inhibition of human tyrosinase inhibitor by verproside from the whole plant of Pseudolysimachion rotundum var. subintegrum
| العنوان: | Potent inhibition of human tyrosinase inhibitor by verproside from the whole plant of Pseudolysimachion rotundum var. subintegrum |
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| المؤلفون: | Sunin Jung, So-Yeun Woo, Mi Hyeon Park, Doo-Young Kim, Su Ui Lee, Sei-Ryang Oh, Mun-Ock Kim, Jinhyuk Lee, Hyung Won Ryu |
| المصدر: | Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 38, Iss 1 (2023) |
| بيانات النشر: | Taylor & Francis Group |
| سنة النشر: | 2023 |
| المجموعة: | Directory of Open Access Journals: DOAJ Articles |
| مصطلحات موضوعية: | Human tyrosinase inhibitor, Verproside, Pseudolysimachion rotundum var. subintegrum, Therapeutics. Pharmacology, RM1-950 |
| الوصف: | Affinity-based ultrafiltration–mass spectrometry coupled with ultraperformance liquid chromatography–quadrupole time-of-flight mass spectrometry was utilised for the structural identification of direct tyrosinase ligands from a crude Pseudolysimachion rotundum var. subintegrum extract. False positives were recognised by introducing time-dependent inhibition in the control for comparison. The P. rotundum extract contained nine main metabolites in the UPLC-QTOF-MS chromatogram. However, four metabolites were reduced after incubation with tyrosinase, indicating that these metabolites were bound to tyrosinase. The IC50 values of verproside (1) were 31.2 µM and 197.3 µM for mTyr and hTyr, respectively. Verproside showed 5.6-fold higher efficacy than that of its positive control (kojic acid in hTyr). The most potent tyrosinase inhibitor, verproside, features a 3,4-dihydroxybenzoic acid moiety on the iridoid glycoside and inhibits tyrosinase in a time-dependent and competitive manner. Among these three compounds, verproside is bound to the active site pocket with a docking energy of −6.9 kcal/mol and four hydrogen bonding interactions with HIS61 and HIS85. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| تدمد: | 1475-6374 1475-6366 |
| العلاقة: | https://doaj.org/toc/1475-6366Test; https://doaj.org/toc/1475-6374Test; https://doaj.org/article/4158c8a98f77452183c883a0469e81beTest |
| DOI: | 10.1080/14756366.2023.2252198 |
| الإتاحة: | https://doi.org/10.1080/14756366.2023.2252198Test https://doaj.org/article/4158c8a98f77452183c883a0469e81beTest |
| رقم الانضمام: | edsbas.84FD5C96 |
| قاعدة البيانات: | BASE |
Full Text Finder | تدمد: | 14756374 14756366 |
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| DOI: | 10.1080/14756366.2023.2252198 |