Solvent polarity controls the helical conformation of short peptides rich in Cα-tetrasubstituted amino acids

Chemistry - A European Journal

Volumn 13, Issue 2, 2007, Pages 407-416

  Bellanda, Massimo ^a   Mammi, Stefano ^a   Geremia, Silvano ^b   Demitri, Nicola ^b   Randaccio, Lucio ^b   Broxterman, Quirinus B ^c   Kaptein, Bernard ^c   Pengo, Paolo ^a   Pasquato, Lucia ^b   Scrimin, Paolo ^a  

^a UNIVERSITY OF PADOVA   (Italy)

^b UNIVERSITY OF TRIESTE   (Italy)

^c DSM RESEARCH   (Netherlands)

Author keywords

Helical structures; NMR spectroscopy; Peptides; Solvent effects; Structure elucidation

Indexed keywords

CIRCULAR DICHROISM (CD) SPECTRA; HELICAL STRUCTURES; PEPTIDES; STRUCTURE ELUCIDATION;

CARBON; CONFORMATIONS; ETHANOL; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; SOLVENTS; X RAY DIFFRACTION ANALYSIS;

AMINO ACIDS;

ACETYL AMINOISOBUTYRYL ALPHA METHYLVALYL AMINOISOBUTYRYL AMINOISOBUTYRYL ALPHA METHYLVALYL AMINOISOBUTYRYL HISTIDINAMIDE; ACETYL-AMINOISOBUTYRYL-ALPHA-METHYLVALYL-AMINOISOBUTYRYL-AMINOISOBUTYRYL-ALPHA-METHYLVALYL-AMINOISOBUTYRYL-HISTIDINAMIDE; AMINO ACID; METHANOL; OLIGOPEPTIDE; SOLVENT; TRIFLUOROETHANOL; UNCLASSIFIED DRUG;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; CIRCULAR DICHROISM; HYDROGEN BOND; NUCLEAR MAGNETIC RESONANCE; PROTEIN SECONDARY STRUCTURE; TEMPERATURE; X RAY CRYSTALLOGRAPHY;

AMINO ACIDS; CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; HYDROGEN BONDING; METHANOL; MODELS, MOLECULAR; MOLECULAR STRUCTURE; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OLIGOPEPTIDES; PROTEIN STRUCTURE, SECONDARY; SOLVENTS; TEMPERATURE; TRIFLUOROETHANOL;

EID: 33846217858     PISSN: 09476539     EISSN: 15213765     Source Type: Journal    
DOI: 10.1002/chem.200600719     Document Type: Article

References (63)

1. a) G. R. Marshall in Intra-Science Chemistry Report, Vol. 5 (Ed.: N. Kharasch), Gordon & Breach, New York, 1971, pp. 305-316;
2. b) C. Toniolo, M. Crisma, F. Formaggio, G. Valle, G. Cavicchioni, G. Précigoux, A. Aubry, J. Kamphuis, Biopolymers 1993, 33, 1061-1072;
3. c) C. Toniolo, M. Crisma, F. Formaggio, C. Peggion, Biopolymers 2001, 60, 396-419;
4. d) E. Mossel, F. Formaggio, G. Valle, M. Crisma, C. Toniolo, M. Doi, T. Ishida, Q. B. Broxterman, J. Kamphuis, Lett. Pept. Sci. 1998, 5, 223-225.
5. a) F. Formaggio, M. Crisma, P. Rossi, P. Scrimin, B. Kaptein, Q. B. Broxterman, J. Kamphuis, C. Toniolo, Chem. Eur. J. 2000, 6, 4498-4504;
6. b) P. Rossi, F. Felluga, P. Tecilla, F. Formaggio, M. Crisma, C. Toniolo, P. Scrimin, J. Am. Chem. Soc. 1999, 121, 6948-6949;
7. c) P. Rossi, F. Felluga, P. Tecilla, F. Formaggio, M. Crisma, C. Toniolo, P. Scrimin, Biopolymers 2000, 55, 496-501;
8. d) C. Sissi, P. Rossi, F. Felluga, F. Formaggio, M. Palumbo, P. Tecilla, C. Toniolo, P. Scrimin, J. Am. Chem. Soc. 2001, 123, 3169-3170;
9. e) A. Scarso, U. Scheffer, M. Göbel, Q. B. Broxterman, B. Kaptein, F. Formaggio, C. Toniolo, P. Scrimin, Proc. Natl. Acad. Sci. USA 2002, 99, 5144-5149.
10. For leading studies see: a) G. R. Marshall, E.E. Hodgkin, D. A. Langs, G. D. Smith, J. Zabrocki, M. T. Leplawy, Proc. Natl. Acad. Sci. USA 1990, 87, 487-491;
11. b) M. L. Smythe, S. E. Huston, G. R. Marshall, J. Am. Chem. Soc. 1993, 115, 11594-11595;
12. c) M. L. Smythe, C. R. Nakaie, G. R. Marshall, J. Am. Chem. Soc. 1995, 117, 10555-10562;
13. d) I. L. Karle, J. L. Flippenanderson, R. Gurunath, P. Balaram, Protein Sei. 1994, 3, 1547-1555;
14. e) S. Vijayalakshmi, R. B. Rao, I. L. Karle, P. Balaram, Biopolymers 2000, 53, 84-98.
15. C. Toniolo, M. Crisma, F. Formaggio, C. Peggion, Q. B. Broxterman, B. Kaptein, Biopolymers 2004, 76, 162-176.
16. a) K. Otoda, Y. Kitagawa, S. Kimura, Y. Imanishi, Biopolymers 1993, 33, 1337-1345;
17. b) M. L. Smythe, S. E. Huston, G. R. Marshall, J. Am. Chem. Soc. 1995, 117, 5445-5452;
18. c) T. S. Yokum, T. J. Gauthier, R. P. Hammer, M. L. McLaughlin, J. Am. Chem. Soc. 1997, 119, 1167-1168;
19. d) I.A. Topol, S. K. Burt, E. Deretey, T.-H. Tang, A. Perczel, A. Rashin, I. G. Csizmadia, J. Am. Chem. Soc. 2001, 123, 6054-6060.
20. G. Hungerford, M. Martinez-Insua, D. J. S. Birch, B. D. Moore, Angew. Chem. 1996, 108, 356-359;
21. Angew. Chem. Int. Ed. Engl. 1996, 35, 326-329.
22. G. Yoder, A. Polese, R. A. G. D. Silva, F. Formaggio, M. Crisma, Q. B. Broxterman, J. Kamphuis, C. Toniolo, T. A. Keiderling, J. Am. Chem. Soc. 1997, 119, 10278-10285.
23. I. L. Karle, P. Balaram, Biochemistry 1990, 29, 6747-6756.
24. A. J. Kirby, Angew. Chem. 1996, 108, 770-790;
25. Angew. Chem. Int. Ed. Engl. 1996, 35, 707-724.
26. a) M. Gerstein, C. Chothia, J. Mol. Biol. 1991, 220, 133-149;
27. b) C. A. McPhalen, M. G. Vincent, D. Picot, J. N. Jansonius, A. M. Lesk, C. Chothia, J. Mol. Biol. 1992, 227, 197-213.
28. P. Pengo, L. Pasquato, S. Moro, A. Brigo, F. Fogolari, Q. B. Broxterman, B. Kaptein, P. Scrimin, Angew. Chem. 2003, 115, 3510-3514;
29. Angew. Chem. Int. Ed. 2003, 42, 3388-3392.
30. a) C. Reichardt, K. Dimroth, Fortschr. Chem. Forsch. 1968, 11, 1;
31. b) C. Reichardt, Solvents and Solvent Effects in Organic Chemistry, VCH, Weinheim, 1988.
32. P. Pengo, Q. B. Broxterman, B. Kaptein, L. Pasquato, P. Scrimin, Langmuir 2003, 19, 2521-2524.
33. S. Mammi, M. Rainaldi, M. Bellanda, E. Schievano, E. Peggion, Q. B. Broxterman, F. Formaggio, M. Crisma, C. Toniolo, J. Am. Chem. Soc. 2000, 122, 11735-11736.
34. M. Bellanda, E. Peggion, R. Bürgi, W. Van Gunsteren, S. Mammi, J. Pept. Res. 2001, 57, 97-106.
35. R.-P. Hummel, C. Toniolo, G. Jung, Angew. Chem. 1987, 99, 1180-1182;
36. Angew. Chem. Int. Ed. Engl. 1987, 26, 1150-1152.
37. C. Toniolo, A. Polese, F. Formaggio, M. Crisma, J. Kamphuis, J. Am. Chem. Soc. 1996, 118, 2744-2745.
38. a) P. Wallimann, R. J. Kennedy, D. S. Kemp, Angew. Chem. 1999, 111, 1377-1379;
39. Angew. Chem. Int. Ed. 1999, 38, 1290-1292;
40. b) P. Wallimann, R. J. Kennedy, J. S. Miller, W. Shalongo, D. S. Kemp, J. Am. Chem. Soc. 2003, 125, 1203-1220.
41. This does not imply that the sequence adopts only one of the two helical conformations. Indeed the two conformations may coexist within the same peptide as also the NMR analysis suggests.
42. a) F. Cordier, S. Grzesiek, J. Am. Chem. Soc. 1999, 121, 1601-1602;
43. b) V. A. Jaravine, A. T. Alexandrescu, S. Grzesiek, Protein Sci. 2001, 10, 943-950;
44. c) M. Bellanda, M. Rainaldi, Q. B. Broxterman, B. Kaptein, F. Formaggio, M. Crisma, S. Mammi, C. Toniolo, Angew. Chem. 2004, 116, 3214-3217;
45. Angew. Chem. Int. Ed. 2004, 43, 3152-3155.
46. K. Wüthrich NMR of Proteins and Nucleic Acids; Wiley: New York 1996.
47. M. Nilges, Proteins Struct. Funct. Genet. 1993, 17, 297-309.
48. a) V. Y. Orekhov, D. M. Korzhnev, T. Diercks, H. Kessler, A. S. Arseniev, J. Biomol. NMR 1999, 14, 345-356;
49. b) R. Armen, D. O. V. Alonso, V. Dagget, Protein Sci. 2003, 12, 1145-1157.
50. 10-helix conformation. See: K. Kitagawa, T. Morita, S. Kimura, Angew. Chem. 2005, 117, 6488-6491;
51. Angew. Chem. Int. Ed. 2005, 44, 6330-6333.
52. We are indebted to Prof. C. Toniolo, University of Padova, for disclosing preliminary data from his laboratory confirming this statement.
53. C. Bartels, T.-H. Xia, M. Billeter, P. Güntert, K. Wüthrich, J. Biomol. NMR 1995, 6, 1-10.
54. A. Bax, R. H. Griffey, B. L. Hawkins, J. Magn. Reson. 1983, 55, 301-315.
55. A. Bax, S. Subramanian, J. Magn. Reson. 1986, 67, 565-569.
56. A. Bax, M. F. Summers, J. Am. Chem. Soc. 1986, 108, 2093-2094.
57. C. Bauer, R. Freeman, T. Frenkiel, J. Keeler, A. J. Shaka, J. Magn. Reson. 1984, 58, 442-457.
58. H. Kessler, C. Griesinger, R. Kerssebaum, K. Wagner, R. R. Ernst, J. Am. Chem. Soc. 1987, 109, 607-609.
59. C. D. Schwieters, J. J. Kuszewski, N. Tjandra, G. M. Clore, J. Magn. Reson. 2003, 160, 65-73.
60. R. Koradi, M. Billeter, K. Wüthrich, J. Mol. Graphics 1996, 14, 51-55.
61. "The CCP4 suite: programs for protein crystallography" Collaborative Computational Project, Number 4, Acta Crystallogr. Sect. D 1994, 50, 760-763.
62. M. C. Burla, M. Camalli, B. Carrozzini, G. L. Cascarano, C. Giacovazzo, G. Polidori, R. Spagna, J. Appl. Crystallogr. 2003, 36, 1103.
63. G. M. Sheldrick SHELXL-97, 1997, University of Götingen (Germany).