74075-20-0Relevant academic research and scientific papers
Studies on the Alkylation of Dipeptide Substrates
Ager, David J.,Froen, Diane E.,Klix, Russell C.,Zhi, Benxin,McIntosh, John M.,Thangarasa, Rasiah
, p. 1975 - 1982 (2007/10/02)
Alkylation of anions derived from dipeptides with a glycine at the C-terminus have been investigated.A hydrocarbon sedition in the N-terminal residue does impart some asymmetric induction.The use of a chiral ester derivative provides the potential for double asymmetric induction and good selectivity.With an aspartyl residue at the N-terminus, problems were encountered due to competing side reactions.The use of an azetidione could circumvent some of these, but the observed induction was not high.
Synthesis and biological activity of a ketomethylene analogue of a tripeptide inhibitor of angiotensin converting enzyme
Almquist,Chao,Ellis,Johnson
, p. 1392 - 1398 (2007/10/02)
An analogue of a tripeptide inhibitor of angiotensin converting enzyme, Bz-Phe-Gly-Pro, has been synthesized in which the amide bond connecting phenylalanine and glycine has been replaced by a ketomethylene group. This nonpeptide analogue, 20, shows more potent converting enzyme inhibiting activity, I50=0.07 μM, than Bz-Phe-Gly-Pro, I50=9.4 μM, or than the orally active D-3-mercapto-2-methylpropanoyl-L-proline (captopril, 1)I50=0.30 μM. Compound 20 has a K(i)of 1.06 x 10-7 and either competitive or noncompetitive enzyme kinetics depending on what substrate is used in the converting enzyme assay. In tests for inhibition of angiotensin I induced contractions in the guinea pig ileum, 20 has one-tenth the activity of 1.
