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

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

Volume: 19 Issue: 26

Author(s): Haizhen A. Zhong, Jack Arbiser and J. Phillip Bowen

Affiliation:

Keywords: MMP-2, MMP-3, MMP-13, rheumatoid arthritis, osteoarthritis, cancer, docking, and zinc binding group.

Abstract: 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.

Cite this article as:

Zhong A. Haizhen, Arbiser Jack and Bowen Phillip J., Selectivity, Binding Affinity, and Ionization State of Matrix Metalloproteinase Inhibitors, Current Pharmaceutical Design 2013; 19 (26) . https://dx.doi.org/10.2174/1381612811319260004