Future challenges facing the development of specific active-site-directed synthetic inhibitors of MMPs

P. Cuniasse, L. Devel, A. Makaritis, F. Beau, D. Georgiadis, M. Matziari, A. Yiotakis, V. Dive*

*Corresponding author for this work

Research output: Contribution to journalShort surveypeer-review

109 Citations (Scopus)

Abstract

Despite a deep knowledge on the 3D-structure of several catalytic domains of MMPs, the development of highly specific synthetic active-site-directed inhibitors of MMPs, able to differentiate the different members of this protease family, remains a strong challenge. Due to the flexible nature of MMP active-site, the development of specific MMP inhibitors will need to combine sophisticated theoretical and experimental approaches to decipher in each MMP the specific structural and dynamic features that can be exploited to obtain the desired selectivity.

Original languageEnglish
Pages (from-to)393-402
Number of pages10
JournalBiochimie
Volume87
Issue number3-4 SPEC. ISS.
DOIs
Publication statusPublished - 2005
Externally publishedYes

Keywords

  • Conformational variability
  • Inhibitor selectivity
  • Inhibitors
  • MMPs
  • Zinc protease

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