83435-61-4Relevant academic research and scientific papers
Continuous Flow Synthesis of ACE Inhibitors From N-Substituted l-Alanine Derivatives
Breen, Christopher P.,Jamison, Timothy F.
, p. 14527 - 14531 (2019/11/03)
A strategy for the continuous flow synthesis of angiotensin converting enzyme (ACE) inhibitors is described. An optimization effort guided by in situ IR analysis resulted in a general amide coupling approach facilitated by N-carboxyanhydride (NCA) activation that was further characterized by reaction kinetics analysis in batch. The three-step continuous process was demonstrated by synthesizing 8 different ACE inhibitors in up to 88 % yield with throughputs in the range of ≈0.5 g h?1, all while avoiding both isolation of reactive intermediates and process intensive reaction conditions. The process was further developed by preparing enalapril, a World Health Organization (WHO) essential medicine, in an industrially relevant flow platform that scaled throughput to ≈1 g h?1.
Method for producing indan derivatives
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, (2008/06/13)
A method for producing an indan derivative represented by the formula: STR1 by condensing an N-(α-alkoxycarbonylaralkyl)-α-amino acid with an N-(indan-2-yl)glycine alkyl or aralkyl ester in the presence of a diphenyl phosphorochloridate, and a method for
Angiotensin-converting enzyme inhibitors: N-substituted glycine derivatives
Suh,Regan,Skiles,et al.
, p. 563 - 570 (2007/10/02)
We report a series of novel dipeptides, which exhibit potent in vitro angiotensin-converting enzyme (ACE) inhibition. These dipeptides embody N-substituted glycine as the COOH terminus amino acid. The dipeptide L-lysyl-N-(2,3-dihydro-1Hinden-5-yl)glycine,
