Selectivity, binding affinity, and ionization state of matrix metalloproteinase inhibitors

Haizhen Andrew Zhong, Jack Arbiser, J. Phillip Bowen

Research output: Contribution to journalArticle

7 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)4701-4713
Number of pages13
JournalCurrent Pharmaceutical Design
Volume19
Issue number26
DOIs
StatePublished - Aug 15 2013

Fingerprint

Matrix Metalloproteinase Inhibitors
Matrix Metalloproteinases
Zinc
Catalytic Domain
Ions

Keywords

  • And zinc binding group
  • Cancer
  • Docking
  • MMP-13
  • MMP-2
  • MMP-3
  • Osteoarthritis
  • Rheumatoid arthritis

ASJC Scopus subject areas

  • Pharmacology
  • Drug Discovery

Cite this

Selectivity, binding affinity, and ionization state of matrix metalloproteinase inhibitors. / Zhong, Haizhen Andrew; Arbiser, Jack; Bowen, J. Phillip.

In: Current Pharmaceutical Design, Vol. 19, No. 26, 15.08.2013, p. 4701-4713.

Research output: Contribution to journalArticle

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