Inhibitors of tripeptidyl peptidase II. 3. Derivation of butabindide by successive structure optimizations leading to a potential general approach to designing …

…, L Zhao, P Bourgeat, C Rose, F Vargas…

文献索引：Ganellin, C. Robin; Bishop, Paul B.; Bambal, Ramesh B.; Chan, Suzanne M. T.; Leblond, Bertrand; Moore, Andrew N. J.; Zhao, Lihua; Bourgeat, Pierre; Rose, Christiane; Vargas, Froylan; Schwartz, Jean-Charles Journal of Medicinal Chemistry, 2005 , vol. 48, # 23 p. 7333 - 7342

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被引用次数: 10

摘要

The cholecystokinin-8 (CCK-8)-inactivating peptidase is a serine peptidase that has been shown to be a membrane-bound isoform of tripeptidyl peptidase II (EC 3.4. 14.10). It cleaves the neurotransmitter CCK-8 sulfate at the Met-Gly bond to give Asp-Tyr (SO3H)-Met-OH+ Gly- Trp-Met-Asp-Phe-NH2. Starting from Val-Pro-NHBu, a dipeptide of submicromolar affinity that had previously been generated to serve as a lead, successive optimization at P3, P1, ...