Vibrational circular-dichroism spectroscopy of homologous cyclic peptides designed to fold into β helices of opposite chirality

Biointerphases

Volumn 6, Issue 1, 2011, Pages 1-7

  Kulp III, John L ^a   Owrutsky, Jeffrey C ^a   Petrovykh, Dmitri Y ^a,b   Fears, Kenan P ^a   Lombardi, Rosina ^c   Nafie, Laurence A ^c   Clark, Thomas D ^a  

^a NAVAL RESEARCH LABORATORY   (United States)

^b Bldg 142   (United States)

^c SYRACUSE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHIRALITY; CHLORINE COMPOUNDS; CIRCULAR DICHROISM SPECTROSCOPY; DICHROISM; SPECTRUM ANALYSIS;

AQUEOUS SOLVENTS; HELICAL CONFORMATION; PEPTIDE ADSORPTION; PEPTIDE BACKBONES; PEPTIDE SECONDARY STRUCTURES; PEPTIDE SEQUENCES; SURFACE ADSORPTION; VIBRATIONAL CIRCULAR DICHROISM SPECTROSCOPY;

PEPTIDES;

CYCLOPEPTIDE;

ARTICLE; CHEMISTRY; CIRCULAR DICHROISM; METABOLISM; METHODOLOGY; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; SPECTROSCOPY; STEREOISOMERISM;

CIRCULAR DICHROISM; PEPTIDES, CYCLIC; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SPECTRUM ANALYSIS; STEREOISOMERISM;

EID: 79952457924     PISSN: 19348630     EISSN: 15594106     Source Type: Journal    
DOI: 10.1116/1.3548075     Document Type: Article

References (53)

1. J. D. Andrade and V. Hlady, Adv. Polym. Sci. 79, 1 (1986).
2. I. Lundström, Prog. Colloid Polym. Sci. 70, 76 (1985).
3. M. Wahlgren and T. Arnebrant, Trends Biotechnol. 9, 201 (1991).
4. O. Mermut, R. L. York, D. C. Phillips, K. R. McCrea, R. S. Ward, and G. A. Somorjai, BioInterphases 1, 5 (2006).
5. D. C. Phillips, R. L. York, O. Mermut, K. R. McCrea, R. S. Ward, and G. A. Somorjai, J. Phys. Chem. C 111, 255 (2007).
6. T. Weidner, J. S. Apte, L. J. Gamble, and D. G. Castner, Langmuir 26, 3433 (2010).
7. H. Kimura-Suda, D. Y. Petrovykh, M. J. Tarlov, and L. J. Whitman, J. Am. Chem. Soc. 125, 9014 (2003).
8. D. Y. Petrovykh, V. Perez-Dieste, A. Opdahl, H. Kimura-Suda, J. M. Sullivan, M. J. Tarlov, F. J. Himpsel, and L. J. Whitman, J. Am. Chem. Soc. 128, 2 (2006).
9. W. C. Johnson, Proteins 7, 205 (1990).
10. M. P. Williamson and J. P. Waltho, Chem. Soc. Rev. 21, 227 (1992).
11. R. W. Woody, Methods Enzymol. 246, 34 (1995).
12. J. T. Yang, C. S. C. Wu, and H. M. Martinez, Methods Enzymol. 130, 208 (1986).
13. T. D. Clark, M. Sastry, C. Brown, and G. Wagner, Tetrahedron 62, 9533 (2006).
14. M. Sastry, C. Brown, G. Wagner, and T. D. Clark, J. Am. Chem. Soc. 128, 10650 (2006).
15. M. Bokvist, F. Lindstrom, A. Watts, and G. Grobner, J. Mol. Biol. 335, 1039 (2004).
16. B. R. Malcolm, Proc. R. Soc. London, Ser. A 305, 363 (1968).
17. G. Vandenbussche, A. Clercx, M. Clercx, T. Curstedt, J. Johansson, H. Jornvall, and J. M. Ruysschaert, Biochemistry 31, 9169 (1992).
18. D. Verreault, V. Kurz, C. Howell, and P. Koelsch, Rev. Sci. Instrum. 81, 063111 (2010).
19. B. Sivaraman, K. P. Fears, and R. A. Latour, Langmuir 25, 3050 (2009).
20. K. P. Fears, B. Sivaraman, G. L. Powell, Y. Wu, and R. A. Latour, Langmuir 25, 9319 (2009).
21. C. R. McMillin and A. G. Walton, J. Colloid Interface Sci. 48, 345 (1974).
22. P. Billsten, M. Wahlgren, T. Arnebrant, J. McGuire, and H. Elwing, J. Colloid Interface Sci. 175, 77 (1995).
23. A. W. P. Vermeer and W. Norde, J. Colloid Interface Sci. 225, 394 (2000).
24. S. L. Burkett and M. J. Read, Langmuir 17, 5059 (2001).
25. M. Shimizu, K. Kazutoshi, H. Morii, K. Mitsui, W. Knoll, and T. Nagamune, Biochem. Biophys. Res. Commun. 310, 606 (2003).
26. A. A. Vertegel, R. W. Siegel, and J. S. Dordick, Langmuir 20, 6800 (2004).
27. M. Lundqvist, P. Nygren, B. H. Jonsson, and K. Broo, Angew. Chem., Int. Ed. 45, 8169 (2006).
28. A. Borics, R. F. Murphy, and S. Lovas, Biopolymers 85, 1 (2007).
29. P. Bour, J. Kim, J. Kapitan, R. P. Hammer, R. Huang, L. Wu, and T. A. Keiderling, Chirality 20, 1104 (2008).
30. J. Hudecová, J. Kapitan, V. Baumruk, R. P. Hammer, T. A. Keiderling, and P. Bour, J. Phys. Chem. A 114, 7642 (2010).
31. J. Kim, J. Kapitan, A. Lakhani, P. Bour, and T. A. Keiderling, Theor. Chem. Acc. 119, 81 (2008).
32. P. Xie and M. Diem, J. Am. Chem. Soc. 117, 429 (1995).
33. W. R. Veatch, E. T. Fossel, and E. R. Blout, Biochemistry 13, 5249 (1974).
34. D. Y. Petrovykh, H. Kimura-Suda, L. J. Whitman, and M. J. Tarlov, J. Am. Chem. Soc. 125, 5219 (2003).
35. C. X. Zhao and P. L. Polavarapu, Biospectroscopy 5, 276 (1999).
36. V. M. Naik and S. Krimm, Biophys. J. 49, 1131 (1986).
37. V. M. Naik and S. Krimm, Biophys. J. 49, 1147 (1986).
38. P. L. Polavarapu and C. X. Zhao, Fresenius' J. Anal. Chem. 366, 727 (2000).
39. C. X. Zhao and P. L. Polavarapu, Biopolymers 62, 336 (2001).
40. C. X. Zhao and P. L. Polavarapu, J. Am. Chem. Soc. 121, 11259 (1999).
41. S. M. Pascal and T. A. Cross, J. Mol. Biol. 226, 1101 (1992).
42. A. S. Arseniev, V. F. Bystrov, V. T. Ivanov, and Y. A. Ovchinnikov, FEBS Lett. 165, 51 (1984).
43. V. F. Bystrov and A. S. Arseniev, Tetrahedron 44, 925 (1988).
44. J. L. Kulp and T. D. Clark, Chem.-Eur. J. 15, 11867 (2009).
45. Y. Chen, A. Tucker, and B. A. Wallace, J. Mol. Biol. 264, 757 (1996).
46. L. A. Nafie, Annu. Rev. Phys. Chem. 48, 357 (1997).
47. S. L. Ma, T. B. Freedman, R. K. Dukor, and L. A. Nafie, Appl. Spectrosc. 64, 615 (2010).
48. -1. We note, furthermore, that for one protein examined, α-chymotrypsin, which comprises mostly β sheet and β turn secondary structures, the VCD spectrum has six identifiable VCD peaks that are similar in frequency and relative intensity to the six VCD peaks of β Val and β Leu that we modeled in the present study.
49. B. A. Wallace, Q. Rev. Biophys. 42, 317 (2009).
50. M. Bieri, C. Gautier, and T. Burgi, Phys. Chem. Chem. Phys. 9, 671 (2007).
51. H. Yao, N. Nishida, and K. Kimura, Chem. Phys. 368, 28 (2010).
52. M. Osawa, Bull. Chem. Soc. Jpn. 70, 2861 (1997).
53. T. R. Jensen, R. P. Van Duyne, S. A. Johnson, and V. A. Maroni, Appl. Spectrosc. 54, 371 (2000).