title: Selectivity, binding affinity, and ionization state of matrix metalloproteinase inhibitors.
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.
authors.affiliation: Department of Chemistry, University of Nebraska at Omaha, DSC362, 6001 Dodge Street, Omaha, NE 68182, USA.
authors.forename: Haizhen A
authors.initials: HA
authors.lastname: Zhong
authors.forename: Jack
authors.initials: J
authors.lastname: Arbiser
authors.forename: J Phillip
authors.initials: JP
authors.lastname: Bowen
mesh_terms: D000595:Amino Acid Sequence; D020782:Matrix Metalloproteinases / Q000187:drug effects* / Q000378:metabolism; D008969:Molecular Sequence Data; D011480:Protease Inhibitors / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D017386:Sequence Homology, Amino Acid
chemical_list: D011480:Protease Inhibitors; D020782:Matrix Metalloproteinases