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Updated: May 15, 2026

Bacterial Expression and Purification of Human Matrix Metalloproteinase-3 using Affinity Chromatography
Published on: March 30, 2022
Selectivity, binding affinity, and ionization state of matrix metalloproteinase inhibitors
Haizhen A Zhong1, Jack Arbiser, J Phillip Bowen
1Department of Chemistry, University of Nebraska at Omaha, DSC362, 6001 Dodge Street, Omaha, NE 68182, USA.
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.
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