Nucleated antiparallel β-sheet that folds and undergoes self-assembly: A template promoted folding strategy toward controlled molecular architectures

Macromolecules

Volumn 29, Issue 1, 1996, Pages 355-366

  Choo, Danny W ^a   Schneider, Joel P ^a   Graciani, Nilsa R ^a   Kelly, Jeffery W ^a  

^a TEXAS A AND M UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0000650678     PISSN: 00249297     EISSN: None     Source Type: Journal    
DOI: 10.1021/ma950703e     Document Type: Article

References (86)

1. (a) Mattice, W. L. Annu. Rev. Biophys. Biophys. Chem. 1989, 18, 93.
2. (b) Yapa, K.; Weaver, D. L.; Karplus, M. Proteins: Struct., Funct., Genet. 1992, 12, 237.
3. (c) Dyson, H. J.; Wright, P. E. Annu. Rev. Biophys. Biophys. Chem. 1991, 20, 519.
4. (d). Liu, Z.-P.; Rizo, J.; Gierasch, L. M. Biochemistry 1994, 33, 134.
5. (a) DeGrado, W. F.; Wasserman, Z. R.; Lear, J. D. Science 1989, 243, 622.
6. (b) Kemp, D. S.; Boyd, J. G.; Muendel, C. C. Nature 1991, 352, 451.
7. (c) Goodman, E. M.; Kim, P. S. Biochemistry 1989, 28, 4343.
8. (d) Lyu, P. C.; Marky, L. A.; Kallenbach, N. R. J. Am. Chem. Soc. 1989, 111, 2733.
9. (e) Poland, D.; Scheraga, H. A. Theory of Helix-Coil Transitions in Biopolymers; Academic Press: New York, 1970.
10. (f) Zimm, B. H.; Bragg, J. J. Chem. Phys. 1959, 31, 526.
11. (a) Kemp, D. S.; Curran, T. P.; Davis, W. M.; Boyd, J. G.; Muendel, C. C. J. Org. Chem. 1991, 56, 6672.
12. (b) DeGrado, W. F.; Lear, J. D. J. Am.. Chem. Soc. 1985, 107, 7684.
13. (c) Zhang, S.; Holmes, T.; Lockshin, C.; Rich, A. Proc. Natl. Acad. Sci. U.S.A. 1993, 90, 3334.
14. (d) Zhang, S.; Lockshin, C.; Cook, R.; Rich, A. Biopolymers 1994, 34, 663.
15. (e) Minor, D. L.; Kim, P. S. Nature 1994, 367, 660.
16. (f) Smith, C. K.; Withka, J. M.; Regan, L. Biochemistry 1994, 33, 5510.
17. (g) Kim, C.; Berg, J. Nature 1993, 362, 267.
18. (a) Hartman, R.; Schwaner, R. C.; Hermans, J, Jr. J. Mol. Biol. 1974, 90, 415.
19. (b) Brack, A.; Orgel, L. E. Nature 1975, 256, 383.
20. (c) Brack, A.; Caille, A. Int. J. Pept. Protein Res. 1978, 11, 128.
21. (d) Brack, A.; Spach, G. J. Am. Chem. Soc. 1981, 103, 6319.
22. (e) Johnson, B. S. J. Pharm. Sci. 1974, 63, 313.
23. (f) Maeda, H.; Ooi, K. Biopolymers 1981, 20, 1549.
24. (g) Maeda, H.; Gatto, Y.; Ikeda, S. Macromolecules 1984, 17, 2031.
25. (h) Maeda, H. Bull. Chem. Soc. Jpn. 1987, 60, 3438.
26. (i) Mattice, W. L.; Lee, E.; Scheraga, H. A. Can. J. Chem. 1985, 63, 140.
27. (j) Rippon, W. B.; Chen, H. H.; Walton, A. G. J. Mol. Biol. 1973, 75, 369.
28. (k) Seipke, G.; Arfmann, H. A.; Wagner, K. G. Biopolymers 1974, 13, 1621.
29. (l) Barbier, B.; Caille, A.; Brack, A. Biopolymers 1984, 23, 2299.
30. (a) Tsang, K. Y.; Diaz, H.; Graciani, N.; Kelly, J. W. J. Am. Chem. Soc. 1994, 116, 3988.
31. (b) Graciani, N. R.; Tsang, K. Y.; McCutchen, S. L.; Kelly, J. W. Bioorg. Med. Chem. 1994, 2, 999.
32. (c) Diaz, H.; Tsang, K. Y.; Choo, D.; Kelly, J. W. Tetrahedron 1993, 49, 3533.
33. (d) Diaz, H.; Tsang, K. Y.; Choo, D.; Espina, J. R.; Kelly, J. W. J. Am. Chem. Soc. 1993, 115, 3790.
34. (e) Diaz, H.; Espina, J. R.; Kelly, J. W. J. Am. Chem. Soc. 1992, 114, 8316.
35. The incorporation of one strategically placed N-methylated amino acid residue into each strand of peptide A affords a monomeric β-sheet structure as discerned from 2D-NMR and far-UV CD studies.
36. For a review on the utility of templates as folding initiators for monomeric protein-like structures, see: Schneider, J. P.; Kelly, J. W. Chem. Rev. 1995, 95, 2169.
37. (a) Tanford, C. The Hydrophobic Effect; Wiley: New York, 1973; p 200.
38. (b) Kaiser, E. T.; Kezdy, F. J. Science 1984, 223, 249.
39. Kaplan, D., Adams, W. W., Farmer, B., Viney, C., Eds. Silk Polymers; ACS Symposium Series 544; American Chemical Society: Washington, D.C., 1994.
40. (a) Krejchi, M. T.; Atkins, E. D. T.; Waddon, A. J.; Fournier, M. J.; Mason, T. L.; Tirrell, D. A. Science 1994, 265, 1427.
41. (b) Beavis, R. C.; Chait, B. T.; Creel, H. S.; Fournier, M. J.; Mason, T. L.; Tirrell, D. A. J. Am. Chem. Soc. 1992, 114, 7584.
42. (c) McGrath, K. P.; Fournier, M. J.; Mason, T. L.; Tirrell, D. A. J. Am. Chem. Soc. 1992, 114, 727.
43. (d) Dougherty, M. J.; Kothakota, S.; Mason, T. L.; Tirrell, D. A. Fournier, M. J. Macromolecules 1993, 26, 1779.
44. (e) Lotz, B.; Keith, H. D. J. Mol. Biol. 1971, 61, 195.
45. (f) Lotz, B. J. Mol. Biol. 1971, 61, 201.
46. (g) Anderson, J. P.; Capello, J.; Martin, D. C. Biopolymers 1994, 34, 1049.
47. (h) Fraser, R. D. B.; MacRae, T. P.; Stewart, F. H. C.; Suzuli, E. J. Mol. Biol. 1965, 11, 706.
48. Manuscripts in ref 9.
49. (a) Glenner, G. G.; Ein, D.; Eanes, E. D.; Bladen, H. A.; Terry, W.; Page, D. L. Science 1971, 174, 712.
50. (b) Kirschner, D. A.; Abraham, C.; Selkoe, D. J. Proc. Natl. Acad. Sci. U.S.A. 1986, 83, 503.
51. (c) Halverson, K.; Fraser, P. E.; Kirschner, D. A.; Lansbury, P. T. Biochemistry 1990, 29, 2639.
52. Replacement of the Lys-3 and Lys-12 residues in peptide A by Thr also affords a pH independent β-sheet structure under identical conditions.
53. Data are shown in the supplementary material.
54. (a) Goto, Y.; Takahashi, N.; Fink, A. Biochemistry 1990, 29, 3480.
55. (b) Goto, Y.; Calciano, L. J.; Fink, A. Proc. Natl. Acad. Sci. U.S.A. 1990, 87, 573.
56. (c) Goto, Y.; Nishikiori, S. J. Mol. Biol. 1991, 218, 387.
57. (d) Goto, Y.; Hagihara, Y. Biochemistry 1992, 31, 732.
58. (e) Goto, Y.; Aimoto, S. J. Mol. Biol. 1991, 218, 387.
59. Djerde, D. T.; Schmuchler, G.; Fritz, J. S. J. Chromatogr. 1980, 187, 35.
60. (b) Gregor, H. P.; Belle, J.; Marcus, R. A. J. Am. Chem. Soc. 1955, 77, 2713.
61. Collins, K. D.; Washabaugh, M. W. Q. Rev. Biophys. 1985, 18, 323.
62. (a) Dill, K. A.; Chan, H. S. Proc. Natl. Aca. Sci. U.S.A. 1990, 87, 6388.
63. (b) Evans, P. A.; Topping, K. D.; Wollfson, D. N.; Dobson, C. M. Proteins: Struct., Funct., Genet. 1991, 9, 248.
64. (c) Garvey, E. P.; Swank, J.; Matthews, C. R. Proteins: Struct., Funct., Genet. 1989, 6, 259.
65. (d) Lumb, K. J.; Kim, P. S. J. Mol. Biol. 1994, 236, 412.
66. (e) Rose, G. D.; Roy, S. Proc. Natl. Acad. Sci. U.S.A. 1980, 77, 4643.
67. (f) Neri, D.; Billeter, M.; Wider, G.; Wüthrich, K. Science 1992, 257, 1559.
68. (g) Topping, K. D.; Evans, P. A.; Dobson, C. M. Proteins 1991, 9, 246.
69. (a) Ralston, G. Introduction to Analytical Ultracentrifugation; Beckman Instruments: Fullerton, CA, 1993; p 86.
70. (b) Adams, E. T., Jr.; Tang, L. H.; Sarquis, J. L.; Barlow, G. H.; Norman, W. M. In Physical Aspects of Protein Interactions; Catsimpoolas, Ed.; Elsevier-North Holland: New York, 1978; pp 1-55.
71. (a) Marsh, R. E.; Corey, R. B.; Pauling, L. Acta Crystallogr. 1955, 8, 710.
72. (b) Geddes, A. J.; Parker, K. D.; Atkins, E. D. Y.; Beighton, E. J. Mol. Biol. 1968, 32, 343.
73. Caputo, C. B.; Fraser, P. E.; Sobel, I.; Kirschner, D. A. Arch. Biochem. Biophys. 1992, 292, 199.
74. (a) Cooper, J. H. Lab. Invest. 1974, 31, 232.
75. (b) Glenner, G. G.; Eanes, E. D.; Page, D. L. J. Histochem. Cytochem. 1972, 20, 821.
76. (c) Hunk, W. E.; Pettegrew, J. W.; Abraham, D. J. J. Histochem. Cytochem. 1989, 37, 1273.
77. (d) Klunk, W. E.; Pettegrew, J. W. J. Histochem. Cytochem. 1989, 37, 1293.
78. (e) Puchtler, H.; Sweat, F.; Levine, M. J. Histochem. Cytochem. 1962, 10, 355.
79. (f) Turnell, W. G.; Finch, J. T. J. Mol. Biol. 1992, 227, 1205.
80. Wolman, M.; Bubis, J. J. Histochemie 1965, 4, 351.
81. Chait, B. T.; Kent, S. B. H. Science 1992, 257, 1885, and references cited therein.
82. Schmid, F. X. In Protein Structure: a Practical Approach; Creighton, T. E., Ed.; IRL Press: New York, 1989; p 251.
83. Pace, C. N.; Shirley, B. A. In Protein Structure: a Practical Approach; Creighton, T. E., Ed.; IRL Press: New York, 1989; p 311.
84. Robinson, D. G.; Ehlers, U.; Herken, R.; Herrmann, B.; Mayer, F.; Schurmann, F.-W. Methods of Preparation for Electron Microscopy: An Introduction for the Biomedical Sciences; Springer-Verlag: Berlin, 1987.
85. This figure was prepared with MolScript, see: Kraulis, P. T. J. Appl. Crystallogr. 1991, 24, 946.
86. Tam, J. P.; Merrifield, R. B. In The Peptides; Analysis, Synthesis and Biology; Udenfriend, S., Meienhofer, J., Eds.; Academic Press: New York, 1987; pp 185-244.