Metal complexes as artificial proteases: toward catalytic drugs

Current Opinion in Chemical Biology

Volumn 12, Issue 2, 2008, Pages 207-213

  Suh, Junghun ^a   Chei, Woo Suk ^a  

^a Seoul National University   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

COBALT; METAL COMPLEX; METALLOPROTEINASE; OLIGOMER; OLIGOPEPTIDE; PROTEINASE;

AMYLOIDOSIS; BINDING SITE; CATALYST; CHEMICAL REACTION; ENZYME ACTIVE SITE; HYDROLYSIS; OXIDATION; REVIEW;

CATALYSIS; HYDROLYSIS; METALLOPROTEASES; METALS; OLIGOPEPTIDES; PROTEINS;

EID: 43049120207     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpa.2008.01.028     Document Type: Review

References (39)

1. Suh J. Synthetic artificial peptidases and nucleases using macromolecular catalytic systems. Acc Chem Res 36 (2003) 562-570. This review describes synthetic artificial peptidases and nucleases that adopt macromolecular catalyst-substrate complexes.
2. Chei W.S., and Suh J. Peptide- or protein-cleaving agents based on metal complexes. Prog Inorg Chem 55 (2007) 79-142. This review discusses hydrolytic or oxidative cleavage of peptide bonds by various types of metal complexes.
3. Ishii M., Matsumura S., and Toshima K. Target-selective degradation of oligosaccharides by a light-activated small-molecule-lectin hybrid. Angew Chem Int Ed 46 (2007) 8396-8399
4. Schepartz A., and Cuenoud B. Site-specific cleavage of the protein calmodulin using a trifluoperazine-based affinity reagent. J Am Chem Soc 112 (1990) 3247-3249
5. Hoyer D., Cho H., and Schultz P.G. New strategy for selective protein cleavage. J Am Chem Soc 112 (1990) 3249-3250
6. Gallagher J., Zelenko O., Walts A.D., and Sigman D.S. Protease activity of 1,10-phenanthroline-copper(I) targeted scission of the catalytic site of carbonic anhydrase. Biochemistry 37 (1998) 2096-2104
7. Gokhale N.H., and Cowan J.A. Inactivation of human angiotensin converting enzyme by copper peptide complexes containing ATCUN motifs. Chem Commun (2005) 5916-5918
8. Gokhale N.H., and Cowan J.A. Metallopeptide-promoted inactivation of angiotensin-converting enzyme and endothelin-converting enzyme 1: toward dual-action therapeutics. J Inorg Biol Chem 11 (2006) 937-947
9. Suh J. Model studies of metalloenzymes involving metal ions as Lewis acid catalysts. Acc Chem Res 25 (1992) 273-279
10. 2 hydrolyzes both dipeptides and proteins. J Am Chem Soc 117 (1995) 7015-7016
11. Takasaki B.K., Kim J.H., Rubin E., and Chin J. Determination of the equilibrium constant for coordination of an amide carbonyl to a metal complex in water. J Am Chem Soc 115 (1993) 1157-1159
12. Jang B.B., Lee K.-P., Min D.-H., and Suh J. Immobile artificial metalloproteinase containing both catalytic and binding groups. J Am Chem Soc 120 (1998) 12008-12016
13. Jang B, Suh J: Kinetic studies on proteolysis by Co(III) complex of cyclen. Bull Kor Chem Soc 2008, 29:202-204.
14. Hettich R., and Schneider H.-J. Cobalt(III) polyamine complexes as catalysts for the hydrolysis of phosphate esters and of DNA. A measurable 10 million-fold rate increase. J Am Chem Soc 119 (1997) 5638-5647
15. Jeon J.W., Son S.J., Yoo C.E., Hong I.S., Song J.B., and Suh J. Protein-cleaving catalyst selective for protein substrate. Org Lett 4 (2002) 4155-4158. This paper reports the first target-selective protein-cleaving catalysts which have been synthesized by using myoglobin as the target protein.
16. Jeon J.W., Son S.J., Yoo C.E., Hong I.S., and Suh J. Toward protein-cleaving catalytic drugs: artificial protease selective for myoglobin. Bioorg Med Chem 11 (2003) 2901-2910
17. Chae P.S., Kim M.-S., Jeung C.-S., Lee S.D., Park H., Lee S.Y., and Suh J. Peptide-cleaving catalyst selective for peptide deformylase. J Am Chem Soc 127 (2005) 2396-2397. This paper reports the first artificial protease selective for a disease-related protein which has been synthesized by using peptide deformylase as the target protein. Peptide deformylase is a target for designing antibiotics.
18. Ravi Rajagopalan P.T., Grimme S., and Pei D. Characterization of cobalt(II)-substituted peptide deformylase: function of the metal ion and the catalytic residue Glu-133. Biochemistry 39 (2000) 779-790
19. Selkoe D.J. Alzheimer's disease: genes, proteins, and therapy. Physiol Rev 81 (2001) 741-766
20. Hardy J., and Selkoe D.J. The amyloid hypothesis of Alzheimer's disease: progress and problems in the road to therapeutics. Science 297 (2002) 353-356
21. Tanzi R.E. The synaptic Aβ hypothesis of Alzheimer's disease. Nat Neurosci 8 (2005) 977-979
22. Snyder E.M., Nong T., Almeida C.G., Paul S., Moran T., Choi E.Y., Nairn A.C., Salter M.W., Lombroso P.J., Gouras G.K., et al. Regulation of NMDA receptor trafficking by amyloid-β. Nat Neurosci 8 (2005) 1051-1058
23. 1-42 oligomer - a homogenous and stable neuropathological protein in Alzheimer's disease. J Neurochem 95 (2005) 834-847
24. Lesné S., Koh M.T., Kotilinek L., Kayed R., Glabe C.G., Yang A., Gallagher M., and Ashe K.H. A specific amyloid-β protein assembly in the brain impairs memory. Nature 440 (2006) 352-357
25. Bitan G., Kirkitadze M.D., Lomakin A., Vollers S.S., Benedek G.B., and Teplow D.B. Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways. Proc Natl Acad Sci U S A 100 (2003) 330-335
26. Schenk D., Barbour R., Dunn W., Gordon G., Grajeda H., Guido T., Hu K., Huang J., Johnson-Wood K., Khan K., et al. Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse. Nature 400 (1999) 173-177
27. DeMattos R.B., Bales K.R., Cummins D.J., Dodart J.-C., Paul S.M., and Holtzman D.M. Peripheral anti-Aβ antibody alters CNS and plasma Aβ clearance and decreases brain Aβ burden in a mouse model of Alzheimer's disease. Proc Natl Acad Sci U S A 98 (2001) 8850-8855
28. Dobson C.M. In the footsteps of alchemists. Science 304 (2004) 1259-1262
29. Cohen T., Frydman-Marom A., Rechter M., and Gazit E. Inhibition of amyloid fibril formation and cytotoxicity by hydroxyindole derivatives. Biochemistry 45 (2006) 4727-4735
30. Choi D.S., Wang D., Yu G.-q., Zhu G., Kharazia V.N., Paredes J.P., Chang W.S., Deitchman J.K., Mucke L., and Messing R.O. PKCε increases endothelin converting enzyme activity and reduces amyloid plaque pathology in transgenic mice. Proc Natl Acad Sci U S A 103 (2006) 8215-8220
31. Suh J., Yoo S.H., Kim M.G., Jeong K., Ahn J.Y., Kim M.-S., Chae P.S., Lee T.Y., Lee J., Lee J., et al. Cleavage agents for soluble oligomers of amyloid β peptides. Angew Chem Int Ed 46 (2007) 7064-7067. This paper reports the first artificial proteases selective for oligomers of amyloidogenic peptides by using amyloid β peptides as the targets. Oligomers of amyloid β peptides are neurotoxic intermediates for Alzheimer's disease.
32. Kim M.-S., Jeon J.W., and Suh J. Angiotensin-cleaving catalysts: conversion of N-terminal aspartate to pyruvate through oxidative decarboxylation catalyzed by Co(III) cyclen. J Biol Inorg Chem 10 (2005) 364-372. This paper describes the first synthetic catalysts for oxidative decarboxylation of N-terminal aspartate residues of oligopeptides. The substrates were angiotensin I and II which are targets for designing drugs for hypertension.
33. In: De Mello W.C. (Ed). Renin Angiotensin System and the Heart (2004), Wiley
34. Bell C.G., Meyre D., Samson C., Boyle C., Lecoeur C., Tauber M., Jouret B., Jaquet D., Levy-Marchal C., Charles M.A., et al. Association of melanin-concentrating hormone receptor 1 5′ polymorphism with early-onset extreme obesity. Diabetes 54 (2005) 3049-3055
35. Kim M.G., Kim M.-S., Lee S.D., and Suh J. Peptide-cleaving catalyst selective for melanin-concentrating hormone: oxidative decarboxylation of N-terminal aspartate catalyzed by Co(III) cyclen. J Biol Inorg Chem 11 (2006) 867-875. This paper describes a synthetic catalyst for oxidative decarboxylation of N-terminal aspartate residue of melanin-concentrating hormone which is a potential target for designing drugs for obesity.
36. Kim M.G., Kim M.-S., Park H., Lee S., and Suh J. Theoretical analysis and prediction of catalysts for oxidative decarboxylation of melanin-concentrating hormone. Bull Kor Chem Soc 27 (2007) 1151-1155
37. Takeuchi T., Böttcher A., Quezada C.M., Simon M.I., Meade T.J., and Gray H.B. Selective inhibition of human α-thrombin by cobalt(III) Schiff base complexes. J Am Chem Soc 120 (1998) 8555-8556
38. In: Parker M.W. (Ed). Protein Toxin Structure (1996), Landes RG Co.
39. Bittan G., Fradinger E.A., Spring S.M., and Teplow D.B. Neurotoxic protein oligomers - what you see is not always what you get. Amyloid 12 (2005) 88-95