1256919-24-0Relevant articles and documents
A conformationally constrained inhibitor with an enhanced potency for β-tryptase and stability against semicarbazide-sensitive amine oxidase (SSAO)
Liang, Guyan,Choi-Sledeski, Yong Mi,Poli, Gregory,Chen, Xin,Shum, Patrick,Minnich, Anne,Wang, Qingping,Tsay, Joseph,Sides, Keith,Cairns, Jennifer,Stoklosa, Gregory,Nieduzak, Thaddeus,Zhao, Zhicheng,Wang, Jie,Vaz, Roy J.
, p. 6721 - 6724 (2010)
A novel β-tryptase inhibitor with a basic benzylamine P1 group, a piperidine-amide linker, and a substituted indole P4 group was discovered. A substitution at 4-indole position was introduced to constrain the conformational flexibility of the inhibitor to the bioactive conformation exhibited by X-ray structures so that entropic penalty was decreased. More importantly, this constrained conformation limited the accessibility of this molecule to anti-targets, especially SSAO, so that an enhanced metabolic profile was achieved.
