367274-58-6Relevant articles and documents
Discovery of diamide compounds as diacylglycerol acyltransferase 1 (DGAT1) inhibitors
Nakajima, Katsumasa,April, Myriam,Brewer, Jason T.,Daniels, Thomas,Forster, Cornelia J.,Gilmore, Thomas A.,Jain, Monish,Kanter, Aaron,Kwak, Youngshin,Li, Jingzhou,McQuire, Les,Serrano-Wu, Michael H.,Streeper, Ryan,Szklennik, Paul,Thompson, James,Wang, Bing
, p. 1245 - 1248 (2016)
Diamide compounds were identified as potent DGAT1 inhibitors in vitro, but their poor molecular properties resulted in low oral bioavailability, both systemically and to DGAT1 in the enterocytes of the small intestine, resulting in a lack of efficacy in vivo. Replacing an N-alkyl group on the diamide with an N-aryl group was found to be an effective strategy to confer oral bioavailability and oral efficacy in this lipophilic diamide class of inhibitors.
Linear oligopeptides. Part 329. Synthesis, characterization and solution conformational analysis of Cα-ethyl, Cα-benzylglycine containing peptides
Formaggio, Fernando,Pantano, Monica,Crisma, Marco,Bonora, Gian Maria,Toniolo, Claudio,Kamphuis, Johan
, p. 1097 - 1102 (2007/10/02)
For the first time a variety of derivatives and terminally blocked model peptides (to the pentapeptide level) of the sterically demanding (αEt)Phe residue have been synthesized (by solution methods) and fully characterized.The results of a solution conformational analysis, performed by using FTIR and 1H NMR spectroscopy, favour the conclusion that (αEt)Phe is a β-turn and helix promoter as strong as (αMe)Phe (Cα-methyl, Cα-benzylglycine) but more efficient than the Phe parent amino acid.In addition, a CD study of Nα-para-bromobenzoylated peptides suggests that the relationship between (αEt)Phe chirality and the screw sense of the turn and helical structures that are formed is the same as that found for (αMe)Phe peptides, i.e.L-amino acids give left-handed helicities.Interestingly, this relationship is opposite to that exhibited by protein amino acids, including Phe.
