Pluripotentialities of a quenched fluorescent peptide substrate library: Enzymatic detection, characterization, and isoenzymes differentiation

Analytical Biochemistry

Volumn 419, Issue 2, 2011, Pages 95-105

  Poras, Hervé ^a   Ouimet, Tanja ^a   Orng, Sou Vinh ^a   Dangé, Emilie ^a   Fournié Zaluski, Marie Claude ^a   Roques, Bernard P ^a  

^a Pharmaleads   (France)

Author keywords

High throughput screening; Proteases; Pyrenylalanine; Quenched fluorescent substrate; Synthetic substrate library

Indexed keywords

AMINO ACIDS; FLUORESCENCE; ISOENZYMES; METABOLITES;

ENZYMATIC DETECTION; FLUORESCENT PEPTIDES; HIGH THROUGHPUT SCREENING; NATURAL AMINO ACIDS; PROTEASES; PYRENYLALANINE; SPECIFIC SUBSTRATES; SYNTHETIC SUBSTRATES;

SUBSTRATES;

4 NITRO PHENYLALANINE; AMINO ACID; ASPARTIC PROTEINASE; CYSTEINE PROTEINASE; GELATINASE B; KALLIKREIN; MATRILYSIN; MEMBRANE METALLOENDOPEPTIDASE; METALLOPROTEINASE; NEPRILYSIN 1; NEPRILYSIN 2; PAPAIN; PEPTIDE; PROTEINASE INHIBITOR; PYRENYLALANINE; SERINE PROTEINASE; TRYPSIN; UNCLASSIFIED DRUG;

ARTICLE; DEPROTECTION REACTION; DRUG SYNTHESIS; FLUORESCENCE; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HIGH THROUGHPUT SCREENING; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; ULTRAVIOLET SPECTROSCOPY;

EID: 80054064692     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2011.08.016     Document Type: Article

References (55)

1. C. Southan A genomic perspective on human proteases FEBS Lett. 498 2001 214 218
2. C. Southan A genomic perspective on human proteases as drug targets Drug Discovery Today 6 2001 681 688
3. G.B.J. Mancini Long-term use of angiotensin-converting enzyme inhibitors to modify endothelial dysfunction: a review of clinical investigations Clin. Invest. Med. 23 2000 144 161
4. A.J. Scheen Pharmacokinetics of dipeptidylpeptidase-4-inhibitors, Diabetes Obes. Metab. 12 2010 648 658
5. M.J.G. Farthing Antisecretory drugs for diarrheal disease J. Dig. Dis. 24 2006 47 58
6. I. Perez-Valero, and J.R. Arribas Protease inhibitor monotherapy Curr. Opin. Infect. Dis. 24 2011 7 11
7. P. Wu, and L. Brand Resonance energy transfer: methods and applications Anal. Biochem. 218 1994 1 13
8. J. Szollosi, S. Damjanovich, and L. Matyus Application of fluorescence resonance energy transfer in the clinical laboratory: routine and research Cytometry 34 1998 159 179
9. A. Yaron, A. Carmel, and E. Katchalski-Katzir Intramolecularly quenched fluorogenic substrates for hydrolytic enzymes Anal. Biochem. 95 1979 228 235
10. A. Carmel, and A. Yaron An intramolecularly quenched fluorescent tripeptide as a fluorogenic substrate of angiotensin-1-converting enzyme and of dipeptidyl carboxypeptidase Eur. J. Biochem. 87 1978 265 273
11. C.G. Knight Fluorimetric assays of proteolytic enzymes Methods Enzymol. 248 1995 18 34
12. J.L. Harris, B.J. Backes, B.F. Leonetti, S. Mahrus, J.A. Ellman, and C.J. Craik Rapid and general profiling of protease specificity by using combinatorial fluorogenic substrate libraries Proc. Natl. Acad. Sci. USA 97 2000 7754 7759
13. M. Meldal, I. Svendsen, K. Breddam, and F.I. Auzanneau Portion-mixing peptide libraries of quenched fluorogenic substrates for complete subsite mapping of endoprotease specificity Proc. Natl. Acad. Sci. USA 91 1994 3314 3318
14. J.J. Peterson, and C.F. Meares Cathepsin substrates as cleavable peptide linkers in bioconjugates selected from a fluorescence quench combinatorial library Bioconjugate Chem. 9 1998 618 626
15. P.M. St Hilaire, M. Willert, M.A. Juliano, L. Juliano, and M. Meldal Fluorescence-quenched solid phase combinatorial libraries in the characterization of cysteine protease substrate specificity J. Comb. Chem. 1 1999 509 523
16. G. Rossé, E. Kueng, M.G.P. Page, V. Schauer-Vukasinovic, T. Giller, H.W. Lahm, P. Hunziker, and D. Schlatter Rapid identification of substrates for novel proteases using a combinatorial peptide library J. Comb. Chem. 2 2000 461 466
17. J.M. Soleilhac, F. Cornille, L. Martin, C. Lenoir, M.C. Fournié-Zaluski, and B.P. Roques A sensitive and rapid fluorescence-based assay for determination of tetanus toxin peptidase activity Anal. Biochem. 241 1996 120 127
18. N. Luciani, H. de Rocquigny, S. Turcaud, A. Romieu, and B.P. Roques Highly sensitive and selective fluorescentt assays for rapid screening of endothelin-converting enzyme inhibitors Biochem. J. 356 2001 813 819
19. 1 subsite of neprilysin: a joined molecular modeling and site-directed mutagenis study Proteins: Struct. Funct. Genet. 39 2000 365 371
20. A. Akbar, G.S.K.K. Reddy, M.N.L. Nalam, S.G. Anjum, H. Cao, C.A. Schiffer, and T.M. Rana Structure-based design, synthesis, and structure-activity relationship of HIV-1 protease inhibitors incorporating phenyloxazolidinones J. Med. Chem. 53 2010 7699 7708
21. C. Oefner, A. D'Arcy, M. Hennig, F.K. Winkler, and G.E. Dale Structure of human neutral endopeptidase (neprilysin) complexed with phosphoramidon J. Mol. Biol. 296 2000 341 349
22. M. Debela, P. Hess, V. Magdolen, N.M. Schechter, T. Steiner, R. Huber, W. Bode, and P. Goettig Chymotryptic specificity determinants in the 1.0 structure of the zinc-inhibited human tissue kallikrein 7 Proc. Natl. Acad. Sci. USA 104 2007 16086 16091
23. J. Cai, J. Robinson, S. Belshaw, K. Everett, X. Fradera, M. van Zeeland, L. van Berkom, P. van Rijnbergen, L. Popplestone, and M. Baugh Trifluoromethylphenyl as P2 for ketoamide-based cathepsin S inhibitors Bioorg. Med. Chem. Lett. 20 2010 6890 6894
24. B.P. Roques, N. Luciani, M.C. Fournié-Zaluski, H. de Rocquigny, Fluorescence detection of proteases and peptidases, US Patent 7169574.
25. B.P. Roques, C. Anne, Peptide substrate recognized by type BoNT/B botulin toxin and use for determination thereof for assaying and/or detecting said toxin or the corresponding inhibitors, US Patent 7160982.
26. C. Anne, F. Cornille, C. Lenoir, and B.P. Roques High-throughput fluorogenic assay for determination of botulinum type B neurotoxin proteases activity Anal. Biochem. 291 2001 253 261
27. M.C. Fournié-Zaluski, B.P. Roques, Fluorescent peptide substrates for botulinum toxin A and their use in screening for inhibitors of the toxin metalloproteinase activity, US Patent 7875436.
28. H. Poras, T. Ouimet, S.-V. Orng, M.C. Fournié-Zaluski, M.R. Popoff, and B.P. Roques Detection and quantification of botulinum neurotoxin type A by a novel rapid in vitro fluorimetric assay Appl. Environ. Microbiol. 75 2009 4382 4390
29. T. Ouimet, S.-V. Orng, H. Poras, K. Gagnidze, L.A. Devi, M.C. Fournié-Zaluski, and B.P. Roques Identification of an endothelin-converting-enzyme-2 specific fluorigenic substrate and development of an in vitro and ex vivo enzymatic assay J. Biol. Chem. 285 2010 34390 34400
30. A. Furka, F. Sebestyen, M. Asgedom, and G. Dibo General method for rapid synthesis of multicomponent peptide mixtures Int. J. Pept. Protein Res. 37 1991 487 493
31. M. Aubry, A. Berteloot, A. Beaumont, B.P. Roques, and P. Crine The use of a monoclonal antibody for the rapid purification of kidney neutral endopeptidase ("enkephalinase") solubilized in octyl glucoside Biochem. Cell Biol. 65 1987 398 404
32. C.G. Knight, F. Willenbrock, and G. Murphy A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases FEBS Lett. 296 1992 263 266
33. O. Oishi, S. Yamashita, M. Ohno, S. Lee, G. Sugihara, and N. Nishino Peculiar photophysical properties of a conformationally proximal pyrene-pair Chem. Phys. Lett. 269 1997 530 534
34. I. Schechter, and A. Burger On the size of the active site in proteases I. Papain Biochem. Biophys. Res. Commun. 27 1967 157 162
35. R.L. Melo, L.C. Alves, E. Del Nery, L.C. Juliano, and M.A. Juliano Synthesis and hydrolysis by cysteine and serine proteases of short internally quenched fluorogenic peptides Anal. Biochem. 293 2001 71 77
36. A.R. Lima, F.M. Alves, P.F. Angelo, D. Andrade, M. Blaber, L. Juliano, and M.A. Juliano S1′ and S2′ subsite specificities of human plasma kallikrein and tissue kallikrein 1 for the hydrolysis of peptides derived from the bradykinin domain of human kininogen Biol. Chem. 389 2008 1487 1494
37. J. Tang Specificity of pepsin and its dependence on a possible hydrophobic binding site Nature 199 1963 1094 1095
38. J. Antal, G. Pal, B. Asboth, Z. Buzas, A. Patthy, and L. Graf Specificity assay of serine proteinases by reverse-phase high-performance liquid chromatography analysis of competiting oligopeptide substrate library Anal. Biochem. 288 2001 156 167
39. R. Menard, A.C. Storer, Papain, in: Barrett A.J., Rawlings N.D., Woessner J.F. (Eds.), Handbook of Proteolytic Enzymes, Elsevier Academic Press, pp. 1125-1128.
40. H.G. Krausslich, R.H. Ingraham, M.T. Skoog, E. Wimmer, P.V. Pallai, and C.A. Carter Activity of purified biosynthetic proteinase of human immunodeficiency virus on natural substrates and synthetic peptides Proc. Natl. Acad. Sci. USA 86 1989 807 811
41. L.B. Hersh, and K. Morihara Comparaison of the subsite specificity of the mammalian neutral endopeptidase 24.11 (enkephalinase) to the bacterial neutral endopeptidase thermolysin J. Biol. Chem. 261 1986 6433 6437
42. 2)Phe-β-Ala, a specific fluorogenic substrate for neutral endopeptidase 24-11 Anal. Biochem. 219 1994 87 95
43. B.P. Roques, F. Noble, V. Daugé, M.C. Fournié-Zaluski, and A. Beaumont Neutral endopeptidase 24.11, structure, inhibition and experimental and clinical pharmacology Pharmacol. Rev. 45 1993 85 146
44. B.F. Le Bonniec, T. Myles, T. Johnson, C.G. Knight, C. Tapparelli, and S.R. Stone Characterization of the P′2 and P′3 specificities of thrombin using fluorescence-quenched substrates and mapping the subsites by mutagenesis Biochemistry 35 1996 7114 7122
45. R.A. Mumford, A.W. Strauss, J.C. Powers, P.A. Pierzchala, N. Nishino, and M. Zimmerman A zinc metalloendopeptidase associated with dog pancreatic membranes J. Biol. Chem. 255 1980 2227 2230
46. T. Ouimet, P. Facchinetti, C. Rose, M. Bonhomme, C. Gros, and J.C. Schwartz Neprilysin II: a putative novel metalloprotease and its isoforms in CNS and testis Biochem. Biophys. Res. Commun. 271 2000 565 570
47. K. Ikeda, N. Emoto, S.B. Rahorjo, Y. Nurhantani, K. Saiki, M. Yokohama, and M. Matsuo Molecular identification and characterization of novel membrane-bound metalloprotease, the soluble secreted form of which hydrolyses a variety of vasoactive peptides J. Biol. Chem. 274 1999 32469 32477
48. G. Ghaddar, A.F. Ruchon, M. Carpentier, M. Marcinkiewicz, N.G. Seidah, P. Crine, L. Desgroseillers, and G. Boileau Molecular cloning and biochemical characterization of a new mouse testis soluble-zinc-metallopeptidase of the neprilysin family Biochem. J. 347 2000 419 429
49. S. Voisin, D. Rognan, C. Gros, and T. Ouimet A three-dimensional model of the neprilysin active site based on the X-ray structure of neprilysin. Identification of residues involved in substrate hydrolysis and inhibitor bonding of neprilysin II J. Biol. Chem. 279 2004 46172 46181
50. G. Tiraboschi, N. Jullian, V. Thery, S. Antonczak, M.C. Fournié-Zaluski, and B.P. Roques A three-dimensional construction of the active site (region 507-749) of human neutral endopeptidase (EC.3.4.24.11) Protein Eng. 12 1999 141 149
51. C. Oefner, B.P. Roques, M.C. Fournie-Zaluski, and G.E. Dale Structural analysis of neprilysin with various specific and potent inhibitors Acta Crystallogr. D. Biol. Crystallogr. 60 2004 392 396
52. H. Sun, R.C. Panicker, and Q.S. Yao Activity based fingerprint of proteases using FRET peptides Biopolymers 88 2007 141 149
53. A.D. Thomas, S.P. Francis, S. Ratcliffe, J.N. Ede, C. Kay, G. Wayne, L.S. Martin, K. Moore, and A. Amour A broad-spectrum fluorescence-based peptide library for the rapid identification of protease substrates Proteomics 6 2006 2112 2120
54. R.A. Lew, N. Tochon-Danguy, C.A. Hamilton, K.M. Stewart, M.I. Aguilar, and A.I. Smith Quenched fluorescent substrate-based peptidase assays Methods Mol. Biol. 298 2005 143 150
55. Z.W. Lai, I. Hanchapola, and A.I. Smith Quenched fluorescent peptide substrate Chem. Today 26 2008 18 21