Quantitative correlation of solvent polarity with the α-/3 10-helix equilibrium: A heptapeptide behaves as a solvent-driven molecular spring

Angewandte Chemie - International Edition

Volumn 42, Issue 29, 2003, Pages 3388-3392

  Pengo, Paolo ^b   Pasquato, Lucia ^a,e   Moro, Stefano ^b   Brigo, Alessandro ^b   Fogolari, Federico ^c   Broxterman, Quirinus B ^d   Kaptein, Bernard ^d   Scrimin, Paolo ^b  

^a CNR   (Italy)

^b UNIVERSITY OF PADOVA   (Italy)

^c UNIVERSITY OF VERONA   (Italy)

^d DSM RESEARCH   (Netherlands)

^e UNIVERSITY OF TRIESTE   (Italy)

Author keywords

Circular dichroism; Helical structures; Peptides; Solvent effects

Indexed keywords

CONFORMATIONS; MOLECULAR DYNAMICS;

SOLVENT POLARITY;

SOLVENTS;

HEPTAPEPTIDE; SOLVENT;

ARTICLE; CIRCULAR DICHROISM; CORRELATION COEFFICIENT; EQUILIBRIUM CONSTANT; PROTEIN STRUCTURE; SOLVENT EFFECT;

AMINO ACIDS; CIRCULAR DICHROISM; HYDROGEN BONDING; MODELS, MOLECULAR; MOLECULAR CONFORMATION; OLIGOPEPTIDES; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SOLVENTS; TIME FACTORS;

EID: 0042074618     PISSN: 14337851     EISSN: None     Source Type: Journal    
DOI: 10.1002/anie.200351015     Document Type: Article

References (43)

1. F. B. Scheinerman, C. L. Brooks III, J. Am. Chem. Soc. 1995, 117, 10098.
2. H. W. Long, R. Tycko, J. Am. Chem. Soc. 1998, 120, 7039.
3. a) G. L. Millhauser, Biochemistry 1995, 34, 3873;
4. b) D. J. Barlow, J. M. Thornton, J. Mol. Biol. 1988, 201, 601.
5. C. Toniolo, E. Benedetti, Trends Biochem. Sci. 1991, 16, 350.
6. K. A. Bolin, G. L. Millhauser, Acc. Chem. Res. 1999, 32, 1027.
7. a) M. L. Smythe, S. E. Huston, G. R. Marshall, J. Am. Chem. Soc. 1995, 117, 5445;
8. b) T. S. Yokum, T. J. Gauthier, R. P. Hammer, M. L. McLaughlin, J. Am. Chem. Soc. 1997, 119, 1167;
9. c) 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.
10. G. Hungerford, M. Martinez-Insua, D. J. S. Birch, B. D. Moore, Angew. Chem. 1996, 108, 356; Angew. Chem. Int. Ed. Engl. 1996, 35, 326.
11. G. Hungerford, M. Martinez-Insua, D. J. S. Birch, B. D. Moore, Angew. Chem. 1996, 108, 356; Angew. Chem. Int. Ed. Engl. 1996, 35, 326.
12. 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.
13. Histidine has been introduced for the catalysis of transacylation reactions; see P. Pengo, Q. B. Broxterman, B. Kaptein, L. Pasquato, P. Scrimin, Langmuir 2003, 19, 2521.
14. a) C. Toniolo, M. Crisma, F. Formaggio, G. Valle, G. Cavicchioni, G. Précigoux, A. Aubry, J. Kamphuis, Biopolymers 1993, 33, 1061;
15. b) C. Toniolo, M. Crisma, F. Formaggio, C. Peggion, Biopolymers 2001, 60, 396.
16. C. Toniolo, A. Polese, F. Formaggio, M. Crisma, J. Kamphuis, J. Am. Chem. Soc. 1996, 118, 2744.
17. F. Formaggio, M. Crisma, P. Rossi, P. Scrimin, B. Kaptein, Q. B. Broxterman, J. Kamphuis, C. Toniolo, Chem. Eur. J. 2000, 6, 4498.
18. Further support for a highly structured conformation in methanol comes from the ROESY NMR spectrum which shows strong intensities of the cross-peaks, thus highlighting the connectivities between the NH and NH(i+1) protons in the sequence (see the Supporting Information).
19. a) P. Wallimann, R. J. Kennedy, D. S. Kemp, Angew. Chem. 1999, 111, 1377; Angew. Chem. Int. Ed. 1999, 38, 1290;
20. a) P. Wallimann, R. J. Kennedy, D. S. Kemp, Angew. Chem. 1999, 111, 1377; Angew. Chem. Int. Ed. 1999, 38, 1290;
21. b) P. Wallimann, R. J. Kennedy, J. S. Miller, W. Shalongo, D. S. Kemp J. Am. Chem. Soc. 2003, 125, 1203.
22. Z. Dang, J. D. Hirst, Angew. Chem. 2001, 113, 3731; Angew. Chem. Int. Ed. 2001, 40, 3619.
23. Z. Dang, J. D. Hirst, Angew. Chem. 2001, 113, 3731; Angew. Chem. Int. Ed. 2001, 40, 3619.
24. 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.
25. Note that the mean residue ellipticity does not change in the concentration interval 1-0.02 mM, which suggests the absence of any aggregation phenomenon at the operational concentration. We have also established that the His residue does not affect the CD spectrum significantly.
26. a) C. Reichardt, K. Dimroth, Fortschr. Chem. Forsch. 1968, 11, 1;
27. b) C. Reichardt, Solvents and Solvent Effects in Organic Chemistry, VCH, Weinheim, 1988.
28. 10-helical conformation (from 4 to 54 °C, methanol) with no evidence of random-coil formation.
29. H. Langhals, Angew. Chem. 1982, 94, 739; Angew. Chem. Int. Ed. Engl. 1982, 21, 724.
30. H. Langhals, Angew. Chem. 1982, 94, 739; Angew. Chem. Int. Ed. Engl. 1982, 21, 724.
31. S. Dixit, J. Crain, W. C. K. Poon, J. L. Finney, A. K. Soper, Nature 2002, 416, 829.
32. A. Bagno, M. Campulla, M. Pirana, G. Scorrano, S. Stiz, Chem. Eur. J. 1999, 5, 1291.
33. A. Cammers-Goodwin, T. J. Allen, S. L. Oslick, K. F. McClure, J. H. Lee, D. S. Kemp, J. Am. Chem. Soc. 1996, 118, 3082.
34. D.-P. Hong, M. Hoshino, R. Kuboi, Y. Goto, J. Am. Chem. Soc. 1999, 121, 8427.
35. B. R. Brooks, R. E. Bruccoleri, B. D. Olafson, D. J. States, S. Swaminathan, M. Karplus, J. Comput. Chem. 1983, 4, 187.
36. W. L. Jorgensen, J. Chandrasekhar, J. D. Madura, R. W. Impey, M. L. Klein, J. Chem. Phys. 1983, 79, 926.
37. E. Neria, S. Fischer, M. Karplus, J. Chem. Phys. 1996, 105, 1902.
38. R. Koradi, M. Billeter, K. Wüthrich, J. Mol. Graphics 1996, 14, 51.
39. I. L. Karle, P. Balaram, Biochemistry 1990, 29, 6747.
40. a) P. Hanson, G. Martinez, G. Millhauser, F. Formaggio, M. Crisma, C. Toniolo, C. Vita, J. Am. Chem. Soc. 1996, 118, 271;
41. b) P. Hanson, G. Millhauser, F. Formaggio, M. Crisma, C. Toniolo, J. Am. Chem. Soc. 1996, 118, 7618.
42. J. P. Ryckaert, G. Ciccitti, H. J. C. Berendsen, J. Comput. Phys. 1977, 23, 327.
43. Molecular Operating Environment (MOE 2002.03), Chemical Computing Group, Inc, 1255 University St., Suite 1600, Montreal, Quebec, Canada, H3B 3X3.