Small peptide inhibitors of acetyl-peptide hydrolase having an uncommon mechanism of inhibition and a stable bent conformation

Journal of Medicinal Chemistry

Volumn 55, Issue 5, 2012, Pages 2102-2111

  Sandomenico, A ^a   Russo, A ^a   Palmieri, G ^b   Bergamo, P ^c   Gogliettino, M ^b   Falcigno, L ^a,d   Ruvo, M ^a  

^a CNR   (Italy)

^b INSTITUTE OF PROTEIN BIOCHEMISTRY   (Italy)

^c CNR   (Italy)

^d UNIVERSITY OF NAPLES FEDERICO II   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

ACYLAMINO ACID RELEASING ENZYME; ENZYME INHIBITOR; TRIFLUOROACETYLATED TETRAPEPTIDE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CATALYSIS; CELL MEMBRANE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME STRUCTURE; HUMAN; HUMAN CELL; PROTEIN CONFORMATION; STRUCTURE ANALYSIS;

APOPTOSIS; CELL LINE, TUMOR; CELL MEMBRANE PERMEABILITY; CIRCULAR DICHROISM; HUMANS; MOLECULAR DYNAMICS SIMULATION; OLIGOPEPTIDES; PEPTIDE HYDROLASES; PEPTIDE LIBRARY; PROTEASE INHIBITORS; PROTEIN CONFORMATION; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 84858021295     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm2013375     Document Type: Article

References (25)

1. Perrier, J.; Durand, A.; Giardina, T.; Puigserver, A. Catabolism of intracellular N-terminal acetylated proteins: involvement of acylpeptide hydrolase and acylase Biochimie 2005, 87, 673-685
2. Adibekian, A.; Martin, B. R.; Wang, C.; Hsu, K. L.; Bachovchin, D. A.; Niessen, S.; Hoover, H.; Cravatt, B. F. Click-generated triazole ureas as ultrapotent in vivo-active serine hydrolase inhibitors Nat. Chem. Biol. 2011, 7, 469-478
3. Narita, K. Isolation of acetylpeptide from enzymic digests of TMV-protein Biochim. Biophys. Acta 1958, 28, 184-191
4. Forte, G. M.; Pool, M. R.; Stirling, C. J. N-terminal acetylation inhibits protein targeting to the endoplasmic reticulum PLoS Biol. 2011, 9, e1001073
5. Shimizu, K.; Kiuchi, Y.; Ando, K.; Hayakawa, M.; Kikugawa, K. Coordination of oxidized protein hydrolase and the proteasome in the clearance of cytotoxic denatured proteins Biochem. Biophys. Res. Commun. 2004, 324, 140-146
6. Palmieri, G.; Bergamo, P.; Luini, A.; Ruvo, M.; Gogliettino, M.; Langella, E.; Saviano, M.; Hegde, R.; Sandomenico, A.; Rossi, M. Acyl Peptide hydrolase Inhibition as targeted strategy to induce proteasomal dysfunction PLoS One 2011, 6 (10) e25888
7. Orlowski, R. Z.; Kuhn, D. J. Proteasome inhibitors in cancer therapy: lessons from the first decade Clin. Cancer Res. 2008, 14, 1649-1657
8. Landis-Piwowar, K. R.; Milacic, V.; Chen, D.; Yang, H.; Zhao, Y.; Chan, T. H.; Yan, B.; Dou, Q. P. The proteasome as a potential target for novel anticancer drugs and chemosensitizers Drug Resist. Updates 2006, 9, 263-273
9. Scaloni, A.; Jones, W.; Pospischil, M.; Sassa, S.; Schneewind, O.; Popowicz, A. M.; Bossa, F.; Graziano, S. L.; Manning, J. M. Deficiency of acylpeptide hydrolase in small-cell lung carcinoma cell lines J. Lab. Clin. Med. 1992, 120, 546-552
10. Palmieri, G.; Langella, E.; Gogliettino, M.; Saviano, M.; Pocsfalvi, G.; Rossi, M. A novel class of protease targets of phosphatidylethanolamine-binding proteins (PEBP): a study of the acylpeptide hydrolase and the PEBP inhibitor from the archaeon Sulfolobus solfataricus Mol. Biosyst. 2010, 6, 2498-2507
11. Olmos, C.; Sandoval, R.; Rozas, C.; Navarro, S.; Wyneken, U.; Zeise, M.; Morales, B.; Pancetti, F. Effect of short-term exposure to dichlorvos on synaptic plasticity of rat hippocampal slices: involvement of acylpeptide hydrolase and alpha(7) nicotinic receptors Toxicol. Appl. Pharmacol. 2009, 238, 37-46
12. Marasco, D.; Perretta, G.; Sabatella, M.; Ruvo, M. Past and future perspectives of synthetic peptide libraries Curr. Protein Pept. Sci. 2008, 9, 447-467
13. Segel, I. H. Enzyme kinetics; Wiley Interscience: New York, 1975; pp 161-166.
14. Wishart, D. S.; Sykes, B. D.; Richards, F. M. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure J. Mol. Biol. 1991, 222, 311-333
15. Abe, F.; Aoyagi, T. Physiological roles of ectoenzymes indicated by the use of aminopeptidase inhibitors. In Ectopeptidases. CD13/Aminopeptidase N and CD26/Dipeptidylpeptidase IV in Medicine and Biology; Langner, J.; Ansorge, S., Eds.; 2002.
16. Yamaguchi, M.; Kambayashi, D.; Toda, J.; Sano, T.; Toyoshima, S.; Hojo, H. Acetylleucine chloromethyl ketone, an inhibitor of acylpeptide hydrolase, induces apoptosis of U937 cells Biochem. Biophys. Res. Commun. 1999, 263, 139-142
17. Moerschell, R. P.; Hosokawa, Y.; Tsunasawa, S.; Sherman, F. The specificities of yeast methionine aminopeptidase and acetylation of amino-terminal methionine in vivo. Processing of altered iso-1-cytochromes c created by oligonucleotide transformation J. Biol. Chem. 1990, 265, 19638-19643
18. Constam, D. B.; Tobler, A. R.; Rensing-Ehl, A.; Kemler, I.; Hersh, L. B.; Fontana, A. Puromycin-sensitive aminopeptidase. Sequence analysis, expression, and functional characterization J. Biol. Chem. 1995, 270, 26931-26939
19. Wickstrom, M.; Larsson, R.; Nygren, P.; Gullbo, J. Aminopeptidase N (CD13) as a target for cancer chemotherapy Cancer Sci. 2011, 102, 501-508
20. Moore, H. E.; Davenport, E. L.; Smith, E. M.; Muralikrishnan, S.; Dunlop, A. S.; Walker, B. A.; Krige, D.; Drummond, A. H.; Hooftman, L.; Morgan, G. J.; Davies, F. E. Aminopeptidase inhibition as a targeted treatment strategy in myeloma Mol. Cancer Ther. 2009, 8, 762-770
21. Casida, J. E.; Quistad, G. B. Serine hydrolase targets of organophosphorus toxicants Chem. Biol. Interact. 2005, 157-158, 277-283
22. Westley, A. M.; Westley, J. Enzyme inhibition in open systems. Superiority of uncompetitive agents J. Biol. Chem. 1996, 271, 5347-52
23. Fields, G. B.; Noble, R. L. Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids Int. J. Pept. Protein Res. 1990, 35, 161-214
24. Palmieri, G.; Catara, G.; Saviano, M.; Langella, E.; Gogliettino, M.; Rossi, M. First Archaeal PEPB-Serine Protease Inhibitor from Sulfolobus solfataricus with Noncanonical Amino Acid Sequence in the Reactive-Site Loop J. Proteome Res. 2009, 8, 327-334
25. Decker, T.; Lohmann-Matthes, M. L. A quick and simple method for the quantitation of lactate dehydrogenase release in measurements of cellular cytotoxicity and tumor necrosis factor (TNF) activity J. Immunol. Methods 1988, 115, 61-69