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Simple pseudo-dipeptides with a P2' glutamate: a novel inhibitor family of matrix metalloproteases and other metzincins.

Devel L, Beau F, Amoura M, Vera L, Cassar-Lajeunesse E, Garcia S, Czarny B, Stura EA, Dive V
J Biol Chem 287 26647-56 (2012)
Related entries: 3ts4, 3tt4, 3tvc, 4efs

Cited: 17 times
EuropePMC logo PMID: 22689580

Abstract

A series of pseudo-peptides with general formula X-l-Glu-NH(2) (with X corresponding to an acyl moiety with a long aryl-alkyl side chain) have been synthesized, evaluated as inhibitors of matrix metalloproteases (MMPs), and found to display remarkable nanomolar affinity. The loss in potency associated with a substitution of the P(2)' l-glutamate by a l-glutamine corroborates the importance of a carboxylate at this position. The binding mode of some of these inhibitors was characterized in solution and by x-ray crystallography in complex with various MMPs. The x-ray crystal structures reveal an unusual binding mode with the glutamate side chain chelating the active site zinc ion. Competition experiments between these inhibitors and acetohydroxamic acid, a small zinc-binding molecule, are in accord with the crystallographic results. One of these pseudo-dipeptides displays potency and selectivity toward MMP-12 similar to the best MMP-12 inhibitors reported to date. This novel family of pseudo peptides opens new opportunities to develop potent and selective inhibitors for several metzincins.

Articles - 3tsk mentioned but not cited (3)

  1. Simple pseudo-dipeptides with a P2' glutamate: a novel inhibitor family of matrix metalloproteases and other metzincins. Devel L, Beau F, Amoura M, Vera L, Cassar-Lajeunesse E, Garcia S, Czarny B, Stura EA, Dive V. J Biol Chem 287 26647-26656 (2012)
  2. Diversity-guided Lamarckian random drift particle swarm optimization for flexible ligand docking. Li C, Sun J, Palade V. BMC Bioinformatics 21 286 (2020)
  3. Divide-and-conquer strategy for large-scale Eulerian solvent excluded surface. Zhao R, Wang M, Tong Y, Wei GW. Commun Inf Syst 18 299-329 (2018)


Reviews citing this publication (6)

  1. Matrix metalloproteinases as breast cancer drivers and therapeutic targets. Radisky ES, Radisky DC. Front Biosci (Landmark Ed) 20 1144-1163 (2015)
  2. Metalloproteinases and Their Inhibitors: Potential for the Development of New Therapeutics. Raeeszadeh-Sarmazdeh M, Do LD, Hritz BG. Cells 9 E1313 (2020)
  3. Therapeutic Potential of Matrix Metalloproteinase Inhibition in Breast Cancer. Radisky ES, Raeeszadeh-Sarmazdeh M, Radisky DC. J Cell Biochem 118 3531-3548 (2017)
  4. Matrix Metalloproteinases and Tissue Inhibitor of Metalloproteinases in Inflammation and Fibrosis of Skeletal Muscles. Alameddine HS, Morgan JE. J Neuromuscul Dis 3 455-473 (2016)
  5. Regulation and involvement of matrix metalloproteinases in vascular diseases. Amin M, Pushpakumar S, Muradashvili N, Kundu S, Tyagi SC, Sen U. Front Biosci (Landmark Ed) 21 89-118 (2016)
  6. Phosphinic Peptides as Tool Compounds for the Study of Pharmacologically Relevant Zn-Metalloproteases. Georgiadis D, Skoulikas N, Papakyriakou A, Stratikos E. ACS Pharmacol Transl Sci 5 1228-1253 (2022)

Articles citing this publication (8)

  1. Crystallization of bi-functional ligand protein complexes. Antoni C, Vera L, Devel L, Catalani MP, Czarny B, Cassar-Lajeunesse E, Nuti E, Rossello A, Dive V, Stura EA. J Struct Biol 182 246-254 (2013)
  2. Synthesis and in Vitro and in Vivo Evaluation of MMP-12 Selective Optical Probes. Bordenave T, Helle M, Beau F, Georgiadis D, Tepshi L, Bernes M, Ye Y, Levenez L, Poquet E, Nozach H, Razavian M, Toczek J, Stura EA, Dive V, Sadeghi MM, Devel L. Bioconjug Chem 27 2407-2417 (2016)
  3. Discovery of a New Class of Potent MMP Inhibitors by Structure-Based Optimization of the Arylsulfonamide Scaffold. Mori M, Massaro A, Calderone V, Fragai M, Luchinat C, Mordini A. ACS Med Chem Lett 4 565-569 (2013)
  4. Robust design of some selective matrix metalloproteinase-2 inhibitors over matrix metalloproteinase-9 through in silico/fragment-based lead identification and de novo lead modification: Syntheses and biological assays. Adhikari N, Halder AK, Mallick S, Saha A, Saha KD, Jha T. Bioorg Med Chem 24 4291-4309 (2016)
  5. Solvent water interactions within the active site of the membrane type I matrix metalloproteinase. Decaneto E, Vasilevskaya T, Kutin Y, Ogata H, Grossman M, Sagi I, Havenith M, Lubitz W, Thiel W, Cox N. Phys Chem Chem Phys 19 30316-30331 (2017)
  6. Design and Synthesis of Water-Soluble and Potent MMP-13 Inhibitors with Activity in Human Osteosarcoma Cells. Zapico JM, Acosta L, Pastor M, Rangasamy L, Marquez-Cantudo L, Coderch C, Ortin I, Nicolau-Sanus M, Puchades-Carrasco L, Pineda-Lucena A, Majali-Martinez A, Ramos P, de Pascual-Teresa B, Ramos A. Int J Mol Sci 22 9976 (2021)
  7. Identification of Broad-Spectrum MMP Inhibitors by Virtual Screening. Gimeno A, Cuffaro D, Nuti E, Ojeda-Montes MJ, Beltrán-Debón R, Mulero M, Rossello A, Pujadas G, Garcia-Vallvé S. Molecules 26 4553 (2021)
  8. Molecular Dynamics Simulations of Matrix Metalloproteinase 13 and the Analysis of the Specificity Loop and the S1'-Site. Choi JY, Chung E. Int J Mol Sci 24 10577 (2023)


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