Sequence-selective peptide recognition with designed modules

European Journal of Organic Chemistry

Volumn , Issue 1, 2006, Pages 138-153

  Wehner, Mark ^a   Janssen, Dominic ^a   Schäfer, Gerhard ^a   Schrader, Thomas ^a  

^a PHILIPPS UNIVERSITY MARBURG   (Germany)

Author keywords

Amino acids; Molecular recognition; Noncovalent interactions; Peptides; Rational design; Receptors; Sequence selectivity

Indexed keywords

EID: 33845738993     PISSN: 1434193X     EISSN: None     Source Type: Journal    
DOI: 10.1002/ejoc.200500393     Document Type: Article

References (51)

1. M. Famulok, K.-S. Jeong, G. Deslongchamps, J. Rebek Jr., Angew. Chem. 1991, 103, 880-882.
2. S. S. Yoon, W. C. Still, J. Am. Chem. Soc. 1993, 115, 823;
3. C-T. Chen, H. Wagner, W. C. Still, Science 1998, 279, 851-853.
4. Review:W. C. Still, Acc. Chem. Res. 1996, 29, 155-163.
5. H. Wennemers, M. Conza, M. Nold, P. Krattiger, Chem. Eur. J. 2001, 7, 3342-3347.
6. T. Braxmeier, M. Demarcus, T. Fessmann, S. McAteer, J. D. Kilburn, Chem. Eur. J. 2001, 7, 1889-1898.
7. C. Schmuck, M. Heil, ChemBioChem 2003, 4, 1232-1238.
8. M. Sirish, V. A. Chertkov, H.-J. Schneider, Chem. Eur. J. 2002, 8, 1181-1188.
9. T. Mizutani, K. Wada, S. Kitagawa, J. Am. Chem. Soc. 1999, 121, 11425-11431.
10. K. Ariga, A. Kamino, X. Cha, T. Kunitake, Langmuir 1999, 15, 3875-3885.
11. D. H. Williams, B. Bardsley, Angew. Chem. Int. Ed. 1999, 38, 1172-1193.
12. J. M. Gardner, R. O. Hynes, Cell 1985, 42, 439-448.
13. M. D. Pierschbacher, E. Ruoslathi, J. Sundelin, P. Lind, P. A. Peterson, J. Biol. Chem. 1982, 257, 9593-9595.
14. A. Miyauchi, J. Alvarez, E. M. Greenfield, A. Teti, M. Grano, S. Colucci, A. Zambonin-Zallone, F. P. Ross, S. L. Teitelbaum, D. A. Cheresh, K. A. Hruska, J. Biol. Chem. 1991, 266, 369-374.
15. M. H. Helfrich, S. A. Nesbitt, E. L. Dorey, M. A. Horton, J. Bone Miner. Res. 1992, 7, 335-343.
16. M.A. Horton, G.A. Rodan, Integrins as therapeutic targets in bone disease, Boca Raton: CRC Press, 1996.
17. J. Folkman, M. Klagsbrun, Science 1987, 235, 442-447.
18. E. Ruoslathi, M. D. Pierschbacher, Science 1987, 238, 491-497.
19. S. M. Albelda, C. A. Buck, FASEB J. 1990, 4, 2868-2880.
20. R. O. Hynes, A. D. Lander, Cell 1992, 68, 303-322.
21. J. Travis, Science 1993, 260, 906-908.
22. A. B. Smith III, R. Hirschmann, A. Pasternak, R. Akaishi, M. C. Guzman, D. R. Jones, T. P. Keenan, P. A. Sprengeler, P. L. Darke, E. A. Emini, M. K. Holloway, W. A. Schleif, J. Med. Chem. 1994, 37, 215.
23. a) Review: J. S. Nowick, Acc. Chem. Res. 1999, 32, 287-296;
24. b) J. H. Tsai, A. S. Waldman, J. S. Nowick, Bioorg. Med. Chem. 1999, 7, 29-38.
25. D. S. Kemp, B. R. Bowen, C. C. Muendel, J. Org. Chem. 1990, 55, 4650.
26. V. Brandmeier, W. H. B. Sauer, M. Feigel, Helv. Chim. Acta 1994, 77, 70.
27. P. Chitnumsub, W. R. Fiori, H. A. Lashuel, H. Diaz, J. W. Kelly, Bioorg. Med. Chem. 1999, 7, 39-59.
28. H. L. Schenck, S. Gellman, J. Am. Chem. Soc. 1998, 120, 4869.
29. T. Schrader, C. Kirsten, Chem. Commun. 1996, 2089.
30. W. S. Weiner, A. D. Hamilton, Bioorg. Med. Chem. Lett. 1998, 8, 681-686.
31. S. T. Phillips, M. Rezac, U. Abel, M. Kossenjans, P. A. Bartlett, J. Am. Chem. Soc. 2002, 124, 58-66.
32. T. Schrader, M. Wehner, Angew. Chem. 2002, 114, 1827-1831.
33. J. Rebek Jr., Angew. Chem. Int. Ed. Engl. 1990, 29, 245-255.
34. T. Bach, H. Bergmann, K. Harms, J. Am. Chem. Soc. 1999, 121, 10650-10651.
35. S. Shinoda, H. Tsukube, Y. Nishimura, I. Yamazaki, A. Osuka, J. Org. Chem. 1999, 64, 3757-3762.
36. B. Askew, P. Ballester, C. Buhr, K. S. Jeong, S. Jones, K. Parris, K. Williams, J. Rebek, Jr., J. Am. Chem. Soc. 1989, 111, 1082-1090.
37. S. Dey, P. Garner, J. Org. Chem. 2000, 65, 7697-7699.
38. a) T. Yvernault, G. Yvernault, J. C. Bollinger, C. R. Acad. Sci. Paris 1978, 287, 519-521;
39. b) J. Coste, E. Frerot, P. Jouin, J. Org. Chem. 1994, 59, 2436-2446.
40. J. L. Sargent, J. Org. Chem. 1954, 19, 599-607.
41. S. Kubik, J. Am. Chem. Soc. 1999, 121, 5846-5855.
42. MacroModel 7.0, Schrödinger Inc., 2000. Force-field: Amber* and OPLS-AA, solvent: chloroform (Monte-Carlo: 2000 steps; MD: 100 ps, 300 K, snapshots taken every 10 ps).
43. a) H. J. Schneider, R. Kramer, S. Simova, U. Schneider, J. Am. Chem. Soc. 1988, 110, 6442;
44. b) C. S. Wilcox, in: Frontiers in Supramolecular Chemistry (Ed.: H. J. Schneider), Verlag Chemie, Weinheim, 1991, p. 123.
45. a) P. Job, Compt. Rend. 1925, 180, 928;
46. b) M. T. Blanda, J. H. Horner, M. Newcomb, J. Org. Chem. 1989, 54, 4626.
47. J. S. Nowick, S. Insaf, J. Am. Chem. Soc. 1997, 119, 10903;
48. the Ala-coil: K. M. Gernert, M. C. Surles, T. H. LaBean, J. S. Richardson, D. C. Richardson, Protein Sci. 1994, 4, 2252-2260.
49. EPS calculations predicted a notable difference between the electron-rich surfaces in Phe and Trp and the electron-poor surface of the m-nitroaniline in host 5: F.-G. Klärner, J. Panitzky, D. Preda, L. T. Scott, J. Mol. Model. 2000, 5, 318.
50. a) M. Delepierre, C. M. Dobson, F. M. Poulsen, Biochemistry 1982, 21, 4756;
51. b) V. F. Bystrov, Prog. Nucl. Magn. Reson. Spectrosc. 1976, 10, 41.