Chinju, South Korea
Chinju, South Korea

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Seo W.D.,NICS | Ryu Y.B.,Korea Research Institute of Bioscience and Biotechnology | Curtis-Long M.J.,12 New Road | Lee C.W.,Amore Pacific | And 3 more authors.
European Journal of Medicinal Chemistry | Year: 2010

The 4′-(p-toluenesulfonylamino)-4-hydroxychalcone (TSAHC), which bears inhibitory chemotypes for both α-glucosidase and tyrosinase, was evaluated for tyrosinase activity and depigmenting ability relative to compounds designed to only target tyrosianse activity. TSAHC emerged to be a competitive reversible inhibitor of mushroom tyrosinase. More importantly, it was also able to return the melanin content of α-melanocyte stimulated by α-MSH to base levels unlike other inhibitors that only targeted tyrosinase. The Western blot for expression levels of proteins involved in melanogenesis showed that TSAHC significantly decreased three main tyrosinase related protein in melanin biosynthesis, tyrosinase, TRP-1 and TRP-2. © 2010 Elsevier Masson SAS. All rights reserved.

Kim E.-J.,Medical Research Center for Neural Dysfunction | Ryu H.W.,BK21 program | Curtis-Long M.J.,12 New Road | Han J.,Medical Research Center for Neural Dysfunction | And 4 more authors.
Bioorganic and Medicinal Chemistry Letters | Year: 2010

Although it has not been extensively studied, a significant volume of literature suggests that TREK2 will probably turn out to be an important channel in charge of tuning neuronal transmitter and hormone levels. Thus, pharmacological tools which can manipulate this channel, such as selective agonists are essential both in drug design and to further our understanding of this system. Our investigations have shown that sulfonate ('O') chalcone and sulfonamide ('N') chalcones regulate the TREK2 channel in remarkably different ways: sulfonamide chalcone 5 behaved as an inhibitor with an IC 50 of 62 μM, whereas the sulfonate analogue 11 activated TREK2 with EC 50 value of 167 μM. © 2010 Elsevier Ltd. All rights reserved.

Oh K.Y.,BK21 Program | Lee J.H.,NAKDONG River Basin Environmental Office | Curtis-Long M.J.,12 New Road | Cho J.K.,BK21 Program | And 3 more authors.
Food Chemistry | Year: 2010

The seeds of Psoralea corylifolia were extracted into five different polar solvents: chloroform, 50% ethanol in water, ethanol, methanol and water. All extracts were evaluated for glycosidase inhibitory activity. The chloroform extract (CE) showed the lowest IC50 values against α-glucosidase (82.9 μg/ml) and α-mannosidase (132 μg/ml). Chromatography of CE yielded nine phenolic compounds which were identified as isovabachalcone (1), 4′-O-methylbavachalcone (2), isobavachromene (3), corylifolin (4), bavachinin (5), psoralidin (6), neobavaisoflavone (7), corylifol A (8), and bakuchiol (9). All isolated compounds, apart from compound 5, possessed α-glucosidase inhibitory activities. Among them, compounds 6-8 exhibited potent inhibition with IC50s of 13.7, 27.7 and 11.3 μM, respectively. Furthermore, compounds 2 and 6 showed α-mannosidase inhibitory activity. Mechanistic analysis of their inhibition modes against α-glucosidase showed that compounds (6 and 7) were noncompetitive, whereas compound 8 was mixed. Furthermore, the most active glycosidase inhibitors (2, 6-8) were proven to be present in the native seed in high quantities by an HPLC chromatogram. © 2010 Elsevier Ltd. All rights reserved.

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