207286-92-8Relevant academic research and scientific papers
Development of potent and selective phosphinic peptide inhibitors of angiotensin-converting enzyme 2
Mores, Andreas,Matziari, Magdalini,Beau, Fabrice,Cuniasse, Philippe,Yiotakis, Athanasios,Dive, Vincent
, p. 2216 - 2226 (2008/12/20)
Angiotensin-Converting enzyme 2 (ACE2), a recently identified human homologue of angiotensin-converting enzyme, is a zinc metallocarboxypeptidase which may play a unique role in cardiovascular and renal function. Here we report the discovery of potent and
Phosphinic derivatives as new dual enkephalin-degrading enzyme inhibitors: Synthesis, biological properties, and antinociceptive activities
Chen, Huixiong,Noble, Florence,Mothé, Aurélie,Meudal, Hervé,Coric, Pascale,Danascimento, Sophie,Roques, Bernard P.,George, Pascal,Fournié-Zaluski, Marie-Claude
, p. 1398 - 1408 (2007/10/03)
The development of dual inhibitors of the two zinc metallopeptidases, neprilysin (neutral endopeptidase) and aminopeptidase N involved in the inactivation of the opioid peptides, enkephalins, represents an attractive physiological approach in the search f
Design of the first highly potent and selective aminopeptidase N (EC 3.4.11.2) inhibitor
Chen, Huixiong,Roques, Bernard P.,Fournie-Zaluski, Marie-Claude
, p. 1511 - 1516 (2007/10/03)
A series of phosphinic compounds mimicking the transition state of substrates hydrolysed by aminopeptidase N (EC 3.4.11.2) were synthesized. These new compounds have potent inhibitory activities with Ki values in the nanomolar range. These derivatives behave as the most potent APN inhibitors designed to date.
