12 New Road

Driffield, United Kingdom

12 New Road

Driffield, United Kingdom

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Ross H.E.,University of Stirling | Cowie A.,12 New Road
International Journal of Arts and Technology | Year: 2010

The full moon subtends an angle of 0.5°, and occupies about 1/100th of the landscape in a standard photograph. Artists usually draw the moon much larger than this, particularly when low on the horizon. The relatively large appearance near the horizon is known as the moon illusion. We tested children aged 4-12 years and adults aged about 21 years, asking them to draw the apparent size of the moon on a photocopy of a landscape, both near the horizon and high in the sky. The mean ratio of the low to high moons was 1.57, and the size of the illusion did not vary significantly with age. The illusion, like sizeconstancy in the near distance, is well established by age 4. Copyright © 2010 Inderscience Enterprises Ltd.


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.


Ryu H.W.,Gyeongsang National University | Curtis-Long M.J.,12 New Road | Jung S.,Gyeongsang National University | Jin Y.M.,Gyeongsang National University | And 4 more authors.
Bioorganic and Medicinal Chemistry | Year: 2010

This study was designed to gain deeper insights into the molecular properties of natural xanthones as neuraminidase inhibitors. A series of xanthones 1-12 was isolated from the seedcases of Garcinia mangostana and evaluated for bacteria neuraminidase inhibitory activity. Compounds 11 and 12 emerged to be new xanthones (mangostenone F, mangostenone G) which we fully spectroscopically characterized. The IC50 values of compounds 1-12 were determined to range between 0.27-65.7 μM. The most potent neuraminidase inhibitor 10 which has an IC50 of 270 nM features a 5,8-diol moiety on the B ring. Interestingly, structure-activity studies reveal that these xanthones show different kinetic inhibition mechanisms depending upon the arrangement of hydroxyl groups in the B ring. Compound 6 possessing a 6,7-diol motif on the B-ring operated under the enzyme isomerization model (k5 = 0.1144 μM-1 s-1, k6 = 0.001105 s -1, and Kiapp = 7.41 μM), whereas compound 10 possessing a 5,8-diol unit displayed simple reversible slow-binding inhibition (k3 = 0.02294 μM-1 s-1, k4 = 0.001025 s -1, and Kiapp = 0.04468 μM). © 2010 Elsevier Ltd. All rights reserved.


Kim J.Y.,Gyeongsang National University | Lee J.W.,Gyeongsang National University | Kim Y.S.,Gyeongsang National University | Lee Y.,Gyeongsang National University | And 7 more authors.
ChemBioChem | Year: 2010

Competitive glycosidase inhibitors are generally sugar mimics that are costly and tedious to obtain because they require challenging and elongated chemical synthesis, which must be stereo-and regiocontrolled. Here, we show that readily accessible achiral (E)-1-phenyl-3-(4-strylphenyl)ureas are potent competitive a-glucosidase inhibitors. A systematic synthesis study shows that the 1-phenyl moiety on the urea is critical for ensuring competitive inhibition, and substituents on both terminal phenyl groups contribute to inhibition potency. The most potent inhibitor, compound 12 (IC50=8.4 μm, Ki=3.2 μm), manifested a simple slow-binding inhibition profile for α-glucosidase with the kinetic parameters k3=0.005256 μm-1min-1, k4=0.003024 min-1, and Ki app =0.5753 μm. © 2010 Wiley-VCH Verlag GmbH& Co. KGaA, Weinheim.


Yuk H.J.,Gyeongsang National University | Lee J.H.,Gyeongsang National University | Curtis-Long M.J.,12 New Road | Lee J.W.,Gyeongsang National University | And 5 more authors.
Food Chemistry | Year: 2011

The leaves of soybean (Glycine max) were extracted into four different polar solvents: ethylacetate, butanol, ethanol and water. The ethylacetate extract (EE) showed the lowest IC50 value against α-glucosidase (70.1 μg/ml). To investigate the compounds responsible for this effect, activity guided fractionation of soybean leaves by chromatography yielded seven phenolic compounds which were identified as formononetin (1), afromosin (2), coumestrol (3), isotrifoliol (4), phaseol (5), glyceofuran (6) and a new compound, glyceollin V (7). Importantly, coumestrol 3 was not only the most potent component with IC50 = 6.0 μM, but also the most abundant polyphenol in soybean leaves. There was shown to be an increasing inhibition across the developmental stage of the plant, which correlated strongly with an increase in compound 3 in the leaves. In fact, we have shown it can comprise up to 65% of the polyphenols in the leaves by HPLC analysis. © 2010 Elsevier Ltd. All rights reserved.


Kim J.Y.,Gyeongsang National University | Lee W.S.,Korea Research Institute of Bioscience and Biotechnology | Kim Y.S.,Gyeongsang National University | Curtis-Long M.J.,12 New Road | And 3 more authors.
Journal of Agricultural and Food Chemistry | Year: 2011

Cholinesterases are key enzymes that play important roles in cholinergic transmission. Nine flavonoids displaying cholinesterase inhibitory activity were isolated from the root bark of Morus lhou L., a cultivated edible plant. The isolated compounds were identified as a new flavone (1), 5′-geranyl-5,7, 2′,4′-tetrahydroxyflavone (2), kuwanon U (3), kuwanon E (4), morusin (5), morusinol (6), cyclomorusin (7), neocyclomorusin (8), and kuwanon C (9). All compounds apart from compound 6 inhibited cholinesterase enzyme in a dose-dependent manner with Ki values ranging between 3.1 and 37.5 μMand between 1.7 and 19.1 μM against acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) enzymes, respectively. The new compound was charactierized as 5′-geranyl-4′-methoxy-5,7,2′- trihydroxyflavone (1). It showed the most potent inhibitory activity (Ki = 3.1 μM for AChE, Ki = 1.74 μMfor BChE). Lineweaver-Burk and Dixon plots and their secondary replots indicated that flavones (5-9) with prenyl substitution on C-3 were noncompetitive inhibitors, whereas those unsubstituted (1-4) at C-3 were mixed inhibitors of both AChE and BChE. In conclusion, this is the first study to demonstrate that alkylated flavonoids of M. lhou have potent inhibitory activities against AChE and BChE. © 2011 American Chemical Society.


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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