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Bioorg Med Chem. 2006 Nov 1;14(21):7241-57. Epub 2006 Jul 17.

Synthesis and structure activity relationships of novel non-peptidic metallo-aminopeptidase inhibitors.

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Laboratoite de Chimie Organique et Bioorganique, UMR 7015, ENSCMu, F-68093 Mulhouse Cedex, France.


Racemic derivatives of 3-amino-2-tetralone were synthesised and evaluated for their ability to inhibit metallo-aminopeptidase activities. New compounds substituted in position 2 by methyl ketone, substituted oximes or hydroxamic acids as well as heterocyclic derivatives were evaluated against representative members of zinc-dependent aminopeptidases: leucine aminopeptidase (E.C., aminopeptidase-N (E.C., Aeromonas proteolytica aminopeptidase (E.C., and the aminopeptidase activity of leukotriene A(4) hydrolase (E.C. Several compounds showed K(i) values in the low micromolar range against the 'one-zinc' aminopeptidases, while most of them were rather poor inhibitors of the 'two-zinc' enzymes. This interesting selectivity profile may guide the design of new, specific inhibitors of target mammalian aminopeptidases with one active site zinc.

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