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Frank Grams, Hans Brandstetter, Simonetta DAlò, Dagmar Geppert, Hans-Willi Krell, Herbert Leinert, Valeria Livi, Ernesto Menta, Ambrogio Oliva, Gerd Zimmermann

Pyrimidine-2,4,6-Triones: A New Effective and Selective Class of Matrix Metalloproteinase Inhibitors

Matrix metalloproteinases (MMPs) are a family of zinc endopeptidases that have been implicated in various disease processes. Different classes of MMP inhibitors, including hydroxamic acids, phosphinic acids and thiols, have been previously described. Most of these mimic peptides and most likely bind in a similar way to the corresponding peptide substrates. Here we desccribe pyrimidinetriones as a completely new class of metalloprotease inhibitors. While the pyrimidinetrione template is used as the zincchelating moiety, the substituents have been optimized to yield inhibitors comparable in their inhibition efficiency of matrix metalloproteinases to hydroxamic acid derivatives such as batimastat. However, they are much more specific for a small subgroup of MMPs, namely the gelatinases (MMP-2 and MMP-9).

Biological Chemistry, Walter de Gruyter

Print ISSN: 1431-6730
Volume: 382, 08/2001
Pages: 1277 - 1285

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