4.5 Article

Selectivity, Binding Affinity, and Ionization State of Matrix Metalloproteinase Inhibitors

期刊

CURRENT PHARMACEUTICAL DESIGN
卷 19, 期 26, 页码 4701-4713

出版社

BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/1381612811319260004

关键词

MMP-2; MMP-3; MMP-13; rheumatoid arthritis; osteoarthritis; cancer; docking; zinc binding group

资金

  1. Research Corporation for Science Advancement
  2. Abbott Excellence in Chemistry Award
  3. Tripos, Inc.
  4. Gaussian, Inc.

向作者/读者索取更多资源

This review highlights some recent advances in the design and development of matrix metalloproteinase inhibitors, especially those targeting MMP-2, MMP-9, and MMP-13. Various zinc-binding groups and non-zinc-binding groups are discussed. Interactions between residues in the critical S1' specificity pocket and MMP inhibitors are given special attention. The influence of ionization states of hydroxamates and retrohydroxamates on the docking outcome and the presence of zinc ions in the active site are explored in light of enhancing enrichment factors for docking studies. Details are given to structural factors for the development of more selective and more potent MMP inhibitors.

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