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The Solution Structure of 18 residue YH motif Peptide within the Second fas-1 domain of βig-h3
한경두,손우성,김우재,이봉진 한국자기공명학회 2007 Journal of the Korean Magnetic Resonance Society Vol.11 No.1
βig-h3 is an extracellular matrix protein that mediates cell adhesion through interaction with integrins. The 18 residue YH motifs within each fas-1 domain are known to be responsible for the interaction with the αvβ5 integrin, and the synthetic YH motif peptides are known to inhibit endothelial tube formation and reduces the number of blood vessels, and so expected to be an effective inhibitor of angiogenesis. In this study, we solved the 3D structure of the 18 residue YH motif peptide (EALRDLLNNHILKSAMCA; D2 peptide) within the second fas-1 domain of βig-h3 using NMR. The Peptide has α-helix structure at the C terminal region but the N terminal region is flexible. The present structural information may be helpful for developing more effective peptide drug candidate for the treatment of diseases dependent on angiogenesis.
이은진,한경두,신희종,김정우,김종국 ( Eun Jin Lee,Kyung Doo Han,Hee Jong Shin,Jung Woo Kim,Chong Kook Kim ) 한국약제학회 1997 Journal of Pharmaceutical Investigation Vol.27 No.1
N/A To investigate the effect of L-arginine as stabilizing agent for omeprazole, the degradation rate constant of omeprazole in aqueous solution was determined at 30, 40 and 50℃ with various ratios of L-arginine to omeprazole. The pH of omeprazole solutions was also determined. As the amount of L-arginine increased, the pH of omeprazole solution also increased, and the solution appeared to be more stable. The omeprazole in aqueous solution could be stabilized by more than 15:1 molar ratio of L-arginine to omeprazole. The stability of omeprazole in commercial products using L-arginine or sodium phosphate dibasic as stabilizing agent was investigated. Among the commercial products, the omeprazole product prepared with L-arginine (molar ratio of L-arginine to omeprazole, 20:1) was most stable.