Haizhen A. Zhong, Jack Arbiser and J. Phillip Bowen Pages 4701 - 4713 ( 13 )
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.
MMP-2, MMP-3, MMP-13, rheumatoid arthritis, osteoarthritis, cancer, docking, and zinc binding group.
, , Center for Drug Design, Department of Pharmaceutical Sciences, College of Pharmacy and Health Sciences, Mercer University, 3001 Mercer University Drive, Atlanta, GA 30341, USA.