869527-87-7Relevant articles and documents
Optimization of Hydroxyethylamine Transition State Isosteres as Aspartic Protease Inhibitors by Exploiting Conformational Preferences
Bueno, Ana B.,Agejas, Javier,Broughton, Howard,Dally, Robert,Durham, Timothy B.,Espinosa, Juan Félix,González, Rosario,Hahn, Patric J.,Marcos, Alicia,Rodríguez, Ramón,Sanz, Gema,Soriano, José F.,Timm, David,Vidal, Paloma,Yang, Hsiu-Chiung,McCarthy, James R.
, p. 9807 - 9820 (2017/12/26)
NMR conformational analysis of a hydroxyethylamine peptide isostere developed as an aspartic protease inhibitor shows that it is a flexible architecture. Cyclization to form pyrrolidines, piperidines, or morpholines results in a preorganization of the who