Literature

Abstract

Both of aminopeptidase N (APN) and matrix metalloproteinase (MMP) are essential metallopeptidases in the development of tumor invasion and angiogenesis. Novel potent peptidomimetic inhibitors, containing 3-galloylamido-N'-substituted-2,6-piperidinedione-N-acetamide, have been designed and synthesized according to the conformational constraint strategy. The preliminary biological test showed that most of the compounds displayed high inhibitory activity against MMP-2 and low activity against APN except compounds 6 (IC(50)=3.1microM) and 4l (IC(50)=5.2microM) which exhibit similar potency to Bestatin (IC(50)=2.4microM).

DOI： 10.1016/j.bmcl.2006.12.095

Novel 3-galloylamido-N′-substituted-2,6-piperidinedione-N-acetamide peptidomimetics as metalloproteinase inhibitors

Bioorganic & Medicinal Chemistry Letters 2007.0

Novel cyclic-imide peptidomimetics as aminopeptidase N inhibitors. Design, chemistry and activity evaluation. Part I

European Journal of Medicinal Chemistry 2009.0

Design, synthesis and primary activity assay of bi- or tri-peptide analogues with the scaffold l-arginine as amino-peptidase N/CD13 inhibitors

Bioorganic & Medicinal Chemistry 2010.0

Novel potent 2,5-pyrrolidinedione peptidomimetics as aminopeptidase N inhibitors. Design, synthesis and activity evaluation

Bioorganic & Medicinal Chemistry Letters 2012.0

Novel aminopeptidase N (APN/CD13) inhibitors derived from 3-phenylalanyl-N′-substituted-2,6-piperidinedione

Bioorganic & Medicinal Chemistry 2010.0

Design, synthesis and SAR studies of tripeptide analogs with the scaffold 3-phenylpropane-1,2-diamine as aminopeptidase N/CD13 inhibitors