Future challenges facing the development of specific active-site-directed synthetic inhibitors of MMPs - PubMed (original) (raw)
Review
Future challenges facing the development of specific active-site-directed synthetic inhibitors of MMPs
P Cuniasse et al. Biochimie. 2005 Mar-Apr.
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.
Similar articles
- Structural basis for the highly selective inhibition of MMP-13.
Engel CK, Pirard B, Schimanski S, Kirsch R, Habermann J, Klingler O, Schlotte V, Weithmann KU, Wendt KU. Engel CK, et al. Chem Biol. 2005 Feb;12(2):181-9. doi: 10.1016/j.chembiol.2004.11.014. Chem Biol. 2005. PMID: 15734645 - Hydroxamate-based peptide inhibitors of matrix metalloprotease 2.
Jani M, Tordai H, Trexler M, Bányai L, Patthy L. Jani M, et al. Biochimie. 2005 Mar-Apr;87(3-4):385-92. doi: 10.1016/j.biochi.2004.09.008. Biochimie. 2005. PMID: 15781326 - Design and characterization of a metalloproteinase inhibitor-tethered resin for the detection of active MMPs in biological samples.
Hesek D, Toth M, Meroueh SO, Brown S, Zhao H, Sakr W, Fridman R, Mobashery S. Hesek D, et al. Chem Biol. 2006 Apr;13(4):379-86. doi: 10.1016/j.chembiol.2006.01.012. Chem Biol. 2006. PMID: 16632250 - Synthetic active site-directed inhibitors of metzincins: achievement and perspectives.
Yiotakis A, Dive V. Yiotakis A, et al. Mol Aspects Med. 2008 Oct;29(5):329-38. doi: 10.1016/j.mam.2008.06.001. Epub 2008 Jul 9. Mol Aspects Med. 2008. PMID: 18657570 Review. - Crystal structures of MMPs in complex with physiological and pharmacological inhibitors.
Maskos K. Maskos K. Biochimie. 2005 Mar-Apr;87(3-4):249-63. doi: 10.1016/j.biochi.2004.11.019. Biochimie. 2005. PMID: 15781312 Review.
Cited by
- MT1-MMP as a Key Regulator of Metastasis.
Tanaka N, Sakamoto T. Tanaka N, et al. Cells. 2023 Aug 31;12(17):2187. doi: 10.3390/cells12172187. Cells. 2023. PMID: 37681919 Free PMC article. Review. - Phosphinic Peptides as Tool Compounds for the Study of Pharmacologically Relevant Zn-Metalloproteases.
Georgiadis D, Skoulikas N, Papakyriakou A, Stratikos E. Georgiadis D, et al. ACS Pharmacol Transl Sci. 2022 Nov 28;5(12):1228-1253. doi: 10.1021/acsptsci.2c00183. eCollection 2022 Dec 9. ACS Pharmacol Transl Sci. 2022. PMID: 36524013 Free PMC article. Review. - Peptides and Peptidomimetics as Inhibitors of Enzymes Involved in Fibrillar Collagen Degradation.
Ledwoń P, Papini AM, Rovero P, Latajka R. Ledwoń P, et al. Materials (Basel). 2021 Jun 10;14(12):3217. doi: 10.3390/ma14123217. Materials (Basel). 2021. PMID: 34200889 Free PMC article. Review. - Polymerizable Matrix Metalloproteinases' Inhibitors with Potential Application for Dental Restorations.
Laronha H, Carpinteiro I, Portugal J, Azul A, Polido M, Petrova KT, Salema-Oom M, Barahona I, Caldeira J. Laronha H, et al. Biomedicines. 2021 Mar 31;9(4):366. doi: 10.3390/biomedicines9040366. Biomedicines. 2021. PMID: 33807479 Free PMC article. - Matrix Metalloproteinase 13 Inhibitors for Modulation of Osteoclastogenesis: Enhancement of Solubility and Stability.
Knapinska AM, Singh C, Drotleff G, Blanco D, Chai C, Schwab J, Herd A, Fields GB. Knapinska AM, et al. ChemMedChem. 2021 Apr 8;16(7):1133-1142. doi: 10.1002/cmdc.202000911. Epub 2021 Jan 26. ChemMedChem. 2021. PMID: 33331147 Free PMC article.