Accueil > Publications > Recherche par années > Années 2000 > 2002

Inguimbert, N ; Coric, P ; Poras, H ; Meudal, H ; Teffot, F ; Fournie-Zaluski, MC ; Roques, BP

Toward an optimal joint recognition of the S-1 ’ subsites of endothelin converting enzyme-1 (ECE-1), angiotensin converting enzyme (ACE), and neutral endopeptidase (NEP)

Journal of Medicinal Chemistry 45 (7) 1477-1486

par Administrateur - publié le

Abstract :

The formation of vasoconstrictors (e.g., angiotensin II and endothelin) and the inactivation of vasodilators (e.g., bradykinin and atrial natriuretic) by membrane-bound zinc metallopeptidases are key mechanisms in the control of blood pressure and fluid homeostasis. The way in which these peptides modulate physiological functions has been intensively studied. With the aim to develop compounds that can jointly block the three metallopeptidases-neutral endopeptidase (NEP, neprilysin), angiotensin-converting enzyme (ACE), and endothelin-converting enzyme (ECE-1)-we studied the common structural specificity of the S-1’ subsites of these peptidases.