Utilizing reversible copper(II) peptide coordination in a sequence-selective luminescent receptor

Chemistry - A European Journal

Volumn 14, Issue 8, 2008, Pages 2536-2541

  Stadlbauer, Stefan ^a   Riechers, Alexander ^a   Späth, Andreas ^a   König, Burkhard ^a  

^a UNIVERSITY OF REGENSBURG   (Germany)

Author keywords

Chelates; Crown compounds; Fluorescence spectroscopy; Molecular recognition; Peptides

Indexed keywords

AMINATION; AMINES; AMINO ACIDS; AMMONIUM COMPOUNDS; BINDING SITES; COORDINATION REACTIONS; COPPER; COPPER COMPOUNDS; ELECTROLYSIS; ETHERS; LUMINESCENCE; METAL IONS; ORGANIC ACIDS; ORGANIC COMPOUNDS; TITRATION; VOLUMETRIC ANALYSIS;

CHELATES; CROWN COMPOUNDS; FLUORESCENCE SPECTROSCOPY; MOLECULAR RECOGNITION; PEPTIDES;

IONS;

COPPER; CROWN ETHER; PEPTIDE;

AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; SPECTROFLUOROMETRY; SYNTHESIS;

AMINO ACID SEQUENCE; COPPER; CROWN ETHERS; PEPTIDES; SPECTROMETRY, FLUORESCENCE;

EID: 53849101441     PISSN: 09476539     EISSN: 15213765     Source Type: Journal    
DOI: 10.1002/chem.200701442     Document Type: Article

References (54)

1. S. Malena, H.-J. Schneider, Chem. Commun. 1999, 907-908.
2. J. Becerril, A. D. Hamilton, Angew. Chem. 2007, 119, 4555-4557;
3. Angew. Chem. Int. Ed. 2007, 46, 4471-4473.
4. A. Hossain, H.-J. Schneider, J. Am. Chem. Soc. 1998, 120, 11208-11209.
5. a) C. Schmuck, P. Wich, Top. Curr. Chem. 2007, 277, 3-30;
6. b) C. Schmuck, D. Rupprecht, W. Wienand, Chem. Eur. J. 2006 12, 9186-9195;
7. c) C. Schmuck, P. Wich, Angew. Chem. 2006, 118, 4383-4387;
8. Angew. Chem. Int. Ed. 2006, 45, 4277-4281.
9. For recent reviews, see: a) H. Kozlowki, W. Bal, M. Dyba, T. Kowalik-Jankowska, Coord. Chem. Rev. 1999, 84, 319-346;
10. b) I. Sovago, K. Osz, Dalton Trans. 2006, 3841-3854.
11. For a recent general review on the use of reversible coordination in molecular recognition, see: M. Kruppa, B. König, Chem. Rev. 2006, 106, 3520-3560.
12. A. T. Wright, E. V. Anslyn, Org. Lett. 2004, 6, 1341-1344.
13. T. Anai, E. Nakata, Y. Koshi, A. Ojida, I. Hamachi, J. Am. Chem. Soc. 2007, 129, 6232-6239.
14. Recent report: M. J. Kelso, R. L. Beyer, H. N. Hoang, A. S. Lakdawala, J. P. Snyder, W. V. Oliver, T. A. Robertson, T. G. Appleton, D. P. Fairlie, J. Am. Chem. Soc. 2004, 126, 4828-4842.
15. Recent study: E. Gaggelli, H. Kozlowski, D. Valensin, G. Valensin, Mol. BioSyst. 2005, 1, 79-84.
16. a) See references in ref. [5a] and [5b] and H. Kozlowski, T. Kowalik-Jankowska, M. Jezowska-Bojczuk, Coord. Chem. Rev. 2005, 249, 2323-2334; recent reports:
17. b) G. Facchin, E. Kremer, E.J. Baran, E. E. Castellano, O. Piro, J. Ellena, A. J. Costa-Filho, M. H. Torre, H. Maria, Polyhedron 2006, 25, 2597-2604;
18. c) V. Joszai, Z. Nagy, K. Osz, D. Sanna, G. Di Natale, D. La Mendola, G. Pappalardo, E. Rizzarelli, Enrico, I. Sovago, J. Inorg. Biochem. 2006, 100, 1399-1409:
19. d) J. D. Bridgewater, J. Lim, R. W. Vachet, Anal. Chem. 2006, 78, 2432-2438;
20. e) L. E. Valenli, C. P. De Pauli, C. E. Giacomelli, J. Inorg. Biochem. 2006, 100, 192-200;
21. f) T. Kowalik-Jankowska, A. Rajewska, K. Wisniewska, Z. Grzonka, J. Jezierska. J. Inorg. Biochem. 2005, 99, 2282-2291;
22. g) M. Swiatek, D. Valensin, C. Migliorini, E. Gaggelli, G. Valensin, M. Jezowska-Bojczuk, Dalton Trans. 2005, 23, 3808-3813.
23. a) W. Yang, D. Jaramillo, J.J. Gooding, D. B. Hibbert, R. Zhang, G. D. Willen, K.J. Fisher, Chem. Commun. 2001, 1982-1983:
24. b) W. Yang, E. Chow, G. D. Willelt, D. B. Hibberl, J. J. Gooding, Analyst 2003, 128, 712-718.
25. M. D. Shults, D. A. Pearce, B. Imperiali, J. Am. Chem. Soc. 2003, 125, 10591-10597.
26. a) B. R. White, J. A. Holcombe, Talanta 2007, 71, 2015-2020;
27. b) A. Mokhir, A. Kiel, D.-P. Herten, R. Kraemer, Inorg. Chem. 2005, 44, 5661-5666;
28. c) Y. Zheng, X. Cao, J. Orbulescu, V. Konka, F. M. Andreopoulos, S. M. Pham, R. M. Leblanc, Anal. Chem. 2003, 75, 1706-1712.
29. E. C. Long, C. A. Claussen, DNA and RNA recognition and modification by gly-gly-his derived metallopeptides in Small Molecule DNA and RNA Binders (Eds.: M. Demeunynck, C. Bailly, W. D. Wilson), Wiley-VCH, Weinheim, 2003, 88-125.
30. a) Y.-Y. Fang, C. A. Claussen, K. B. Lipkowitz, E. C. Long, J. Am. Chem. Soc. 2006, 128, 3198-3207;
31. b) Y. Jin, M. A. Lewis, N. H. Gokhale, E. C. Long, J. A. Cowan, J. Am. Chem. Soc 2007, 129, 8353-8361.
32. a) G. Brookes, L. D. Pettit, J. Chem. Soc. Dalton Trans. 1975, 2112-2117;
33. b) P. Daniele, O. Zerbinati, R. Aruga, G. Ostacoli, J. Chem. Soc. Dalton Trans. 1988, 1115-1120;
34. c) D. D. Perrin, V. Sharma, J. Chem. Soc. A 1967, 724.
35. a) L. Baolong, L. Bazong, L. Jianping, Z. Yong, Inorg. Chem. Commun. 2003, 6, 725-727;
36. b) L. Baolong, L. Bazong, Z. Xia, Z. Yong, Inorg. Chem. Commun. 2003, 6, 1304-1306;
37. c) Y. Huawa, S. Juen, C. Liaorong, L. Baosheng, Polyhedron 1996, 15, 3891-3895.
38. C. P. Mandl, B. König, J. Org. Chem. 2005, 70, 670-674.
39. M. Kruppa, C. Mandl, S. Miltschitzky, B. König, J. Am. Chem. Soc. 2005, 127, 3362-3365.
40. S. Lata, A. Reichel, R. Brock, R. Tampé, J. Piehler, J. Am. Chem. Soc. 2005, 127, 10205-10215.
41. II ions. The emission intensity of the ligand itself does not change in the presence of the target peptide sequences; see Supporting Information for data on ligand 4 in the presence of GGH.
42. V. Rüdiger, H.-J. Schneider, V. P. Solov'ev, V. P. Kazachenko, O. A. Raevsky, Eur. J. Org. Chem. 1999, 8, 1847-1856.
43. From titration values it was estimated that an emission intensity increase of more than 100% under the experimental conditions corresponds to a binding affinity larger than millimolar.
44. Peptides such as GGH are know to bind copper(II) ions tightly. To ensure that the observed emission increase of 5 in the presence of such a peptide was not caused by NTA-Cu decomplexation, the stability of 5 in the presence of excess GGH was investigated (see Supporting Information). If the copper ion were to be transferred from NTA to the peptide, the emission intensity of ligand 4 should be restored, which is not the case. We therefore conclude that the NTA-Cu complex of 5 is sufficiently stable even in the presence of peptides with high copper affinity.
45. The larger side chain in GIn starts to alter the binding motif.
46. M. Rainer, B. Rode, Inorg. Chim. Acta 1985, 107, 127-132.
47. The enthalphic contributions to the binding processes are similar for both peptides, indicating the same metal ion coordination. The difference in the binding constants is of entropie origin, which may be explained by the desolvatisation of the crown ether unit and the ammonium ion upon aggregate formation (see Supporting Information for data).
48. A. Rigo, A. Corazza, M. L. di Paolo, M. Rossetto, R. Ugolini, M. Scarpa. J. Inorg. Biochem. 2004, 98, 1495-1501.
49. Stability constants of NTA-copper complexes with cysteine have been determine electrophoretically and found to be in the order of log6: B. B. Tewari, J. Chromatogr. A 2006, 1103, 139-144.
50. 0 more difficult. R. M. Krishnan, V. S. Muralidharan, Proceed. Ind. Acad. Sci. Chem. Sci. 1991, 103, 107-118. The redox properties of Cu-NTA complexes in the presence of thiols have not been investigated to the best of our knowledge.
51. Such coordination structures have been suggested for copper(II) NTA cysteine: a) B. B. Tewari, Russ, J. Coord. Chem. 2003, 29, 441-444, and related systems;
52. b) T. H. Cooper, M. J. Mayer, K.-H. Leung, L. A. Ochrymowycz, D. B. Rorabacher, Inorg. Chem. 1992, 31, 3796-3804;
53. c) E. A. Ambundo, M.-V. Deydier, A. J. Grail, N. Aguera-Vega, L. T. Dressel, T. H. Cooper, M. J. Heeg, L. A. Ochrymowycz, D. B. Rorabacher, Inorg. Chem. 1999, 38, 4233-4242;
54. d) E. A. Ambundo, M.-V. Deydier, L. A. Ochrymowycz, D. B. Rorabacher. Inorg. Chem. 2000, 39, 1171-1179.