237394-18-2Relevant academic research and scientific papers
Phosphinic pseudo-tripeptides as potent inhibitors of matrix metalloproteinases: A structure-activity study
Vassiliou, Stamatia,Mucha, Artur,Cuniasse, Philippe,Georgiadis, Dimitris,Lucet-Levannier, Karine,Beau, Fabrice,Kannan, Rama,Murphy, Gillian,Kn?uper, Vera,Rio, Marie-Christine,Basset, Paul,Yiotakis, Athanasios,Dive, Vincent
, p. 2610 - 2620 (1999)
Several phosphinic pseudo-tripeptides of general formula R-XaaΨ(PO2- CH2)Xaa'-Yaa'-NH2 were synthesized and evaluated for their in vitro activities to inhibit stromelysin-3, gelatinases A and B, membrane type-1 matrix metalloproteinase, collagenases 1 and 2, and matrilysin. With the exception of collagenase-1 and matrilysin, phosphinic pseudo-tripeptides behave as highly potent inhibitors of matrix metalloproteinases, provided they contain in P1' position an unusual long aryl-alkyl substituent. Study of structure-activity relationships regarding the influence of the R and Xaa' substituents in this series may contribute to the design of inhibitors able to block only a few members of the matrix metalloproteinase family.
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
