Analogues containing the paramagnetic amino acid TOAC as substrates for angiotensin I-converting enzyme

FEBS Letters

Volumn 581, Issue 13, 2007, Pages 2411-2415

  de Deus Teixeira, Luis Gustavo ^a   Bersanetti, Patrícia Alessandra ^a   Schreier, Shirley ^b   Carmona, Adriana Karaoglanovich ^a   Nakaie, Clovis Ryuichi ^a  

^a FEDERAL UNIVERSITY OF SÃO PAULO   (Brazil)

^b UNIVERSITY OF SÃO PAULO   (Brazil)

Author keywords

Angiotensin I converting enzyme; Angiotensins; Electron spin resonance spectroscopy; Enzymes; Peptides; TOAC

Indexed keywords

2,2,6,6 TETRAMETHYLPIPERIDINE 1 OXYL 4 AMINO 4 CARBOXYLIC ACID; ANGIOTENSIN I; CARBOXYLIC ACID DERIVATIVE; DIGLYCINE; DIPEPTIDYL CARBOXYPEPTIDASE; TYROSINE; UNCLASSIFIED DRUG;

AMINO ACID ANALYSIS; ANIMAL TISSUE; ARTICLE; BIOASSAY; CONTROLLED STUDY; ELECTRON SPIN RESONANCE; ELECTROSPRAY MASS SPECTROMETRY; FLUORESCENCE SPECTROSCOPY; LIQUID CHROMATOGRAPHY; NONHUMAN; PRIORITY JOURNAL; RAT; STEREOSPECIFICITY; STRUCTURE ACTIVITY RELATION;

ANIMALS; CYCLIC N-OXIDES; ELECTRON SPIN RESONANCE SPECTROSCOPY; FEMALE; GUINEA PIGS; ILEUM; KINETICS; MASS SPECTROMETRY; PEPTIDES; PEPTIDYL-DIPEPTIDASE A; RATS; SPECTROMETRY, FLUORESCENCE; SUBSTRATE SPECIFICITY; UTERUS;

EID: 34248578221     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.04.058     Document Type: Article

References (44)

1. Nakaie C.R., Goissis G., Schreier S., and Paiva A.C.M. pH dependence of ESR spectra of nitroxide containing ionizable groups. Braz. J. Med. Biol. Res 14 (1981) 173-180
2. Nakaie C.R., Schreier S., and Paiva A.C.M. Synthesis and properties of spin-labeled angiotensin derivatives. Biochim. Biophys. Acta 742 (1983) 63-71
3. Barany G., and Merrifield R.B. The Peptides Vol. 2 (1980), Academic Press Inc., New York
4. Fields G.B., and Noble R.L. Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids. Int. J. Pept. Prot. Res. 35 (1990) 161-214
5. Rassat A., and Rey P. Nitroxydes. 23. Préparation dàminoacides radicalaires et de leurs sels complexes. Bull. Soc. Chim. Fr. 3 (1967) 815-817
6. Marchetto R., Schreier S., and Nakaie C.R. A novel spin-labeled amino acid derivative for use in peptide synthesis: (9-fluorenylmethyloxycarbonyl) - 2.2.6.6-tetramethylpiperidine-1-oxyl-4-amino-4-carboxylic acid. J. Am. Chem. Soc. 115 (1993) 11042-11043
7. (10)-helical conformation of alanine-based peptides in aqueous solution: an electron spin resonance investigation. J. Am. Chem. Soc. 117 (1995) 10555-10562
8. α,α-disubstituted glycine. J. Pept. Sci. 1 (1995) 45-57
9. McNulty J.C., Silapie J.L., Carnevali M., Farrar C.T., Griffin R.G., Formaggio F., Crisma M., Toniolo C., and Milhauser G.L. Electron spin resonance of TOAC labeled peptides: folding transitions and high frequency spectroscopy. Biopolymers 55 (2000) 479-485
10. D'Amore M., Improta R., and Barone V. Conformational behavior and magnetic properties of a nitroxide amino acid derivatives in vacuo and in aqueous and in aqueous solution. J. Phys. Chem. A 107 (2003) 6264-6269
11. Marsh D. Orientation of TOAC amino-acid spin labels in α-helices and β-strands. J. Magn. Res. 180 (2006) 305-310
12. Bettio A., Gutewort V., Pöppl A., Dinger M.C., Zschörnig O., Arnold K., Toniolo C., and Beck-Sickinger A.G. Electron paramagnetic resonance backbone dynamics studies on spin-labeled neuropeptides Y analogues. J. Peptide Sci. 8 (2002) 671-682
13. Nakaie C.R., Silva E.G., Cilli E.M., Marchetto R., Schreier S., Paiva T.B., and Paiva A.C.M. Synthesis and pharmacological properties of TOAC-labeled angiotensin and bradykinin analogues. Peptides 23 (2002) 65-70
14. Schreier S., Barbosa S.R., Casallanovo F., Vieira R.F.F., Cilli E.M., Paiva A.C.M., and Nakaie C.R. Conformational basis for the biological activity of TOAC-labeled angiotensin II and bradykinin: electron paramagnetic resonance, circular dichroism and fluorescence studies. Biopolymers 74 (2004) 389-402
15. Barbosa S.R., Cilli E.M., Lamy-Freund M.T., Castrucci A.M.L., and Nakaie C.R. First synthesis of a fully active spin-labeled peptide hormone. FEBS Lett. 446 (1999) 45-48
16. Karim C.B., Kirby T.L., Zhang Z., Nesmelov Y., and Thomas D.D. Phospholamban structural dynamics in lipid bilayers probed by a spin label rigidly coupled to the peptide backbone. Proc. Natl. Acad. Sci. USA 101 (2004) 14437-14442
17. α-tetrasubstituted α-amino acid, is an excellent tool in material science and biochemistry. Biopolymers 47 (1998) 153-158
18. Pertinhez T.A., Nakaie C.R., Paiva A.C.M., and Schreier S. Spin-labeled extracellular loop from a seven-transmembrane helix receptor: studies in solution and interaction with model membranes. Biopolymers 42 (1997) 821-829
19. Victor K.G., and Cafiso D.S. Location and dynamics of basic peptides at the membrane interface electron paramagnetic resonance spectroscopy of tetramethyl-piperidine-1-oxyl-4-amino-4-carboxylic acid. Biophys. J. 81 (2001) 2241-2250
20. Inbaraj J.J., Cardon T.B., Laryukhin M., Grosser S.M., and Lorigan G.A. Determining the topology of integral membrane peptides using EPR spectroscopy. J. Am. Chem. Soc. 128 (2006) 9549-9554
21. Cilli E.M., Marchetto R., Schreier S., and Nakaie C.R. Use of spin label EPR spectra to monitor peptide chain aggregation inside resin beads. Tetrahedron Lett. 38 (1997) 517-520
22. Cilli E.M., Marchetto R., Schreier S., and Nakaie C.R. Correlation between the mobility of spin labeled peptide chains and resin salvation: an approach to optimize the synthesis of aggregating sequences. J. Org. Chem. 64 (1999) 9118-9123
23. Oliveira E., Cilli E.M., Miranda A., Jubilut G.N., Alberício F., Andreu D., Paiva A.C.M., Schreier S., Tominaga M., and Nakaie C.R. Monitoring the chemical assembly of a transmembrane bradykinin receptor fragment: correlation between resin solvation, peptide chain mobility and rate of coupling. Eur. J. Org. Chem. 21 (2002) 3686-3694
24. Marchetto R., Cilli E.M., Jubilut G.N., Schreier S., and Nakaie C.R. Determination of site-site distance and site concentration within polymer beads: a combined swelling-electron paramagnetic resonance study. J. Org. Chem. 70 (2005) 4561-4568
25. Corvol P., Willians T.A., and Soubrier F. Peptidyl dipeptidase A: angiotensin I-converting enzyme. Methods in Enzymology vol. 248 (1995), Academic Press
26. Skidgel R.A., and Erdös E.G. Angiotensin converting enzyme (ACE) and neprilysin hydrolyze neuropeptides: a brief history, the beginning and follow-ups to early studies. Peptides 25 (2004) 521-525
27. Acharya K.R., Sturrock E.D., Riordan J.F., and Ehlers M.R.W. ACE revisited: a new target for structure-based drug design. Nat. Rev. Drug. Discov. 2 (2003) 891-902
28. Paul M., Mehr A.P., and Kreutz R. Physiology of local rennin-angiotensin systems. Physiol. Rev. 86 (2006) 747-803
29. Skeggs L.T., Kahn J.R., and Shumway N.P. Preparation and function of the hypertension converting enzyme. J. Exp. Med. 103 (1956) 295-299
30. Young H.Y.T., Erdös E.G., and Levin Y. A dipeptidyl carboxypeptidase that converts angiotensin I and inactivates bradykinin. Biochim. Biophys. Acta 214 (1970) 374-376
31. Paul M., Mehr A.P., and Kreutz R. Physiology of local rennin-angiotensin systems. Physiol. Rev. 86 (2006) 747-803
32. Araújo M.C., Melo R.L., Cesari M.H., Juliano M.A., Juliano L., and Carmona A.K. Peptidase specificity characterization of C- and N-terminal catalytic sites of angiotensin I-converting enzyme. Biochemistry 39 (2000) 8519-8525
33. Zaman M.A., Oparil S., and Calhoun D.A. Drugs targeting the rennin-angiotensin-aldosterone system. Nat. Rev. Drug Discov. 1 (2002) 621-636
34. Bersanetti P.A., Andrade M.C., Casarini D.E., Juliano M.A., Nehinda A.T., Sturrock E.D., Juliano L., and Carmona A.K. Positional-scanning combinatorial libraries of fluorescence resonance energy transfer peptides for defining substrate specificity of the angiotensin I-converting enzyme and development of selective C-domain substrates. Biochemistry 43 (2004) 15729-157736
35. Ehlers M.R.W., and Riordan J.F. Angiotensin-converting enzyme: zinc and inhibitor binding stoichiometries of the aromatic and testis enzymes. Biochemistry 30 (1991) 7118-7126
36. Kivelson D. Theory of ESR linewidths of free radicals. J. Chem. Phys. 33 (1960) 1094-1106
37. Barret J.D., and Sambhi M.P. Simultaneous assay of angiotensin I and II and determination of converting enzyme activity. J. Pharmacol. Exp. Ther. 170 (1969) 326-333
38. Paiva A.C.M., and Paiva T.B. The importance of the N-terminal end of angiotensin II for its pressor and oxytocic activities. Biochem. Pharmacol. 5 (1960) 187-191
39. Marshall G.R., Eilers N., and Vine W. In: Lande S. (Ed). Progress in Peptide Research (1972), Gordon and Breach, New York 15-18
40. Park W.K., Asselin J., and Berlingurt L. In: Lande S. (Ed). Progress in Peptide Research (1972), Gordon and Breach, New York 49-58
41. Angus C.W., Lee H.J., and Wilson I.B. Substrate specificity of hog plasma angiotensin-converting enzyme. Biochim. Biophys. Acta 309 (1973) 169-174
42. Oparil S., Koermer T., and O'Donehue J.N. Structural requirements for substrates and inhibitors of angiotensin I-converting enzyme in vivo and vitro. Circ. Res. 40 (1974) 19-26
43. Bunning P., Budek K., Escher R., and Schonherr E. Characteristic of angiotensin converting enzyme and its role in the metabolism of angiotensin I by endothelium. J. Cardiovasc. Pharmacol. 8 (1986) S52-S57
44. Freed J.H., and Frankel G.K. Theory of linewidths in electron spin resonance spectra. J. Chem. Phys. 39 (1963) 326-348