Conformational polymorphism of the amyloidogenic peptide homologous to residues 113-127 of the prion protein

Biophysical Journal

Volumn 85, Issue 1, 2003, Pages 473-483

  Satheeshkumar, K S ^a   Jayakumar, R ^a  

^a CENTRAL LEATHER RESEARCH INSTITUTE   (India)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; AMYLOID PROTEIN; DODECYL SULFATE SODIUM; OLIGOPEPTIDE; PRION PROTEIN; SOLVENT; TRIFLUOROETHANOL;

ACIDITY; AMINO TERMINAL SEQUENCE; AQUEOUS SOLUTION; ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; CONCENTRATION RESPONSE; CONFORMATIONAL TRANSITION; GENETIC POLYMORPHISM; INFRARED SPECTROSCOPY; IONIC STRENGTH; PH; PRION DISEASE; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; SEQUENCE ANALYSIS; SPECTROSCOPY;

EID: 0038650572     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)74492-0     Document Type: Article

References (68)

1. Albert, J. S., and A. D. Hamilton. 1995. Stabilization of helical domains in short peptides using hydrophobic interactions. Biochemistry. 34:984-990.
2. Baldwin, M. A., F. E. Cohen, and S. B. Prusiner. 1995. Prion protein isoforms, a convergence of biological and structural investigations. J. Biol. Chem. 270:19197-19200.
3. Bodanszky, M., and A. Bodanszky. 1984. The Practice of Peptide Synthesis. Springer-Verlag, New York.
4. Bodkin, M. J., and J. M. Goodfellow. 1996. Hydrophobic solvation in aqueous trifluoroethanol solution. Biopolymers. 39:43-50.
5. Brown, D. R. 1999. Prion protein peptide neurotoxicity can be mediated by astrocytes. J. Neurochem. 73:1105-1113.
6. Brown, D. R. 2000. Prion protein peptides: optimal toxicity and peptide blockade of toxicity. Mol. Cell. Neurosci. 15:66-78.
7. Bruch, M. D., M. M. Dhingra, and L. M. Gierasch. 1991. Side chain-backbone hydrogen bonding contributes to helix stability in peptides derived from an alpha-helical region of carboxypeptidase A. Proteins. Struct. Funct. Genet. 10:130-139.
8. Caughey, B., D. A. Kocisko, G. J. Raymond, and P. T. Lansbury, 1995. Aggregates of scrapie-associated prion protein induce the cell-free conversion of protease-sensitive prion protein to the protease-resistant state. Chem. Biol. 2:807-816.
9. Chakrabartty, A., T. Kortemme, S. Padmanabhan, and R. L. Baldwin. 1993. Aromatic side-chain contribution to far-ultraviolet circular dichroism of helical peptides and its effect on measurement of helix propensities. Biochemistry. 32:5560-5565.
10. Chiti, F., P. Webster, N. Taddei, M. Stefani, G. Ramponi, and C. M. Dobson. 1999. Designing conditions for in vitro formation of amyloid protofilaments and fibrils. Proc. Natl. Acad. Sci. USA. 96:3590-3594.
11. Chou, P. Y., and G. D. Fasman. 1978. Empirical predictions of protein conformation. Annu. Rev. Biochem. 47:251-276.
12. Donne, D. G., J. H. Viles, D. Groth, I. Mehlhorn, T. L. James, F. E. Cohen, S. B. Prusiner, P. E. Wright, and H. J. Dyson. 1997. Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible. Proc. Natl. Acad. Sci. USA. 94:13452-13457.
13. Fasman, G. D. 1996. Theory of circular dichroism of proteins. In Circular Dichroism and the Conformational Analysis of Biomolecules. R. W. Woody, editor. Plenum Press, New York. 55.
14. Forloni, G., N. Angeretti, R. Chiesa, E. Monzani, M. Salmona, O. Bugiani, and F. Tagliavini. 1993. Neurotoxicity of a prion protein fragment. Nature. 362:543-546.
15. Forloni, G., R. Del Bo, N. Angeretti, R. Chiesa, S. Smiroldo, R. Doni, E. Ghibandi, M. Salmona, M. Porro, L. Verga, G. Giaccone, O. Bugiani, and F. Tagliavini. 1994. A neurotoxic prion protein fragment induces rat astroglial proliferation and hypertrophy. Eur. J. Neurosci. 6:1415-1422.
16. Forloni, G., F. Tagliavini, O. Bugiani, and M. Salmona. 1996. Amyloid in Alzheimer's disease and prion-related encephalopathies: studies with synthetic peptides. Prog. Neurobiol. 49:287-315.
17. Gasset, M., M. A. Baldwin, D. H. Lloyd, J. M. Gabriel, D. M. Holtzman, F. Cohen, R. Fletterick, and S. B. Prusiner. 1992. Predicted alpha-helical regions of the prion protein when synthesized as peptides form amyloid. Proc. Natl. Acad. Sci. USA. 89:10940-10944.
18. Gioia, L. D., C. Selvaggini, E. Ghibaudi, L. Diomede, O. Bugiani, G. Forloni, F. Tagliavini, and M. Salomona. 1994. Conformational polymorphism of the amyloidogenic and neurotoxic peptide homologous to residues 106-126 of the prion protein. J. Biol. Chem. 269:7859-7862.
19. Greenfield, N. J., and G. D. Fasman. 1969. Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry. 8:4108-4116.
20. Grob, M., D. K. Wilkins, M. C. Pitkeathly, E. W. Chung, C. Higham, A. Clark, and C. M. Dobson. 1999. Formation of amyloid fibrils by peptides derived from the bacterial cold-shock protein cspB. Protein Sci. 8:1350-1357.
21. Guijarro, J. I., M. Sunde, J. A. Jones, I. D. Campbell, and C. M. Dobson. 1998. Amyloid fibril formation by SH3 domain. Proc. Natl. Acad. Sci. USA. 95:4224-4228.
22. Harrison, P. M., P. Bamborough, V. Daggett, S. B. Prusiner, and F. E. Cohen. 1997. The prion protein problem. Curr. Opin. Struct. Biol. 7:53-59.
23. Hermans, P. H. 1949. Chapter XII. Gels. In Colloid Science, Vol. 2. H. R. Kruyt, editor. Elsevier, Amsterdam. 483-651.
24. Huang, Z., S. B. Prusiner, and F. E. Cohen. 1996a. Scrapie prions: a three-dimensional model of an infectious fragment. Fold. Des. 1:13-19.
25. Huang, Z., S. B. Prusiner, and F. E. Cohen. 1996b. Structures of prion proteins and conformational models for prion diseases. Curr. Top. Microbiol. Immunol. 207:49-67.
26. James, T. L., H. Liu, N. B. Ulyanov, S. Farr-Jones, H. Zhang, D. G. Donne, K. Kaneko, D. Groth, I. Mehlhom, S. B. Prusiner, and F. E. Cohen. 1997. Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform. Proc. Natl. Acad. Sci. USA. 94:10086-10091.
27. Jansanoff, A., and A. R. Fersht. 1994. Quantitative determination of helical propensities from trifluoroethanol titration curves. Biochemistry. 33:2129-2135.
28. 3 -OMe in chloroform and N, N-dimethyl formamide. Langmuir. 16:1489-1496.
29. Katsoyannis, P. G., and G. P. Schwartz. 1977. The synthesis of peptides by homogeneous solution procedures. Methods Enzymol. XLVII:501-578.
30. Kelly, J. W. 1998. The alternative conformation of amyloidogenic proteins and their multi-step assembly pathways. Curr. Opin. Struct. Biol. 8:101-106.
31. Kelly, J. W. 2000. Mechanism of amyloidogenesis. Nat. Struct. Biol. 7:824-826.
32. Kishore, R., S. Raghothama, and P. Balaram. 1987. Cystine peptides: the intramolecular antiparallel beta-sheet conformation of a 20-membered cyclic peptide disulfide. Biopolymers. 26:873-891.
33. Lansbury, P. T., and B. Caughey. 1995. The chemistry of scrapie infection: implications of the "ice 9" metaphor. Chem. Biol. 2:1-5.
34. Laxma Reddy, G., and R. Nagaraj. 1989. Circular dichroism studies on synthetic signal peptides indicate beta-conformation as a common structural feature in highly hydrophobic environment. J. Biol. Chem. 264:16591-16597.
35. Lehrman, S. R., J. L. Tuls, and M. Lund. 1990. Peptide alpha-helicity in aqueous trifluoroethanol: correlations with predicted alpha-helicity and the secondary structure of the corresponding regions of bovine growth hormone. Biochemistry. 29:5590-5596.
36. Levy, Y., and O. M. Becker. 2002. Conformational polymorphism of wild-type and mutant prion proteins: energy landscape analysis. Proteins. 47:458-468.
37. Luidens, M. K., J. Figge, K. Breese, and S. Vajda. 1996. Predicted and trifluoroethanol-induced alpha-helicity of polypeptides. Biopolymers. 39:367-376.
38. Madison, V., and J. Schellman. 1972. Optical activity of polypeptides and proteins. Biopolymers. 11:1041-1076.
39. McKinley, M. P., M. B. Braunfeld, C. G. Bellinger, and S. B. Prusiner. 1986. Molecular characteristics of prion rods purified from scrapie-infected hamster brains. J. Infect. Dis. 154:110-120.
40. McLeish, M. J., K. J. Nielson, L. V. Najbar, J. D. Wade, F. Lin, M. B. Doughty, and D. J. Craik, 1994. Conformation of a peptide corresponding to T4 lysozyme residues 59-81 by NMR and CD spectroscopy. Biochemistry. 33:11174-11183.
41. Merukta, G., W. Lipton, W. Shalongo, S. Park, and E. Stellwagen. 1990. Effect of central-residue replacements on the helical stability of a monomeric peptide. Biochemistry. 29:7511-7515.
42. Myers, J. K., C. Nickpace, and J. M. Scholtz. 1998. Trifluoroethanol effects on helix propensity and electrostatic interactions in the helical peptide from ribonuclease T1. Protein Sci. 7:383-388.
43. Nelson, J. W., and N. R. Kallenbach. 1986. Stabilization of the ribonuclease S-peptide alpha-helix by trifluoroethanol solutions. Proteins. Struct. Funct. Genet. 1:211-217.
44. Pan, K.-M., M. Baldwin, J. Nguyen, M. Gasset, A. Serban, D. Groth, I. Mehlhorn, Z. Huang, R. J. Fletterick, F. E. Cohen, and S. B. Prusiner. 1993. Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins. Proc. Natl. Acad. Sci. USA. 90:10962-10966.
45. Petchanikow, C., G. P. Saborio, L. Anderes, M. J. Frossard, M. I. Olmedo, and C. Soto. 2001. Biochemical and structural studies of the prion protein polymorphism. FEBS Lett. 509:451-456.
46. Pintar, A., A. Chollet, C. Bradshaw, A. Chaffotte, C. Cadieux, M. J. Rooman, K. Hallenga, J. Knowles, M. Goldberg, and S. J. Wodak. 1994. Conformational properties of four peptides corresponding to alpha-helical regions of Rhodospirillum cytochrome c2 and bovine calcium binding protein. Biochemistry. 33:11158-11173.
47. Prusiner, S. B. 1982. Novel proteinaceous infectious particles cause scrapie. Science. 216:136-144.
48. Prusiner, S. B. 1997. Prion diseases and the BSE crisis. Science. 278:245-251.
49. Prusiner, S. B. 1998. Prions. Proc. Natl. Acad. Sci. USA. 95:13363-13383.
50. Prusiner, S. B., M. P. McKinley, K. A. Bowman, D. C. Bolton, P. E. Bendheim, D. F. Groth, and G. G. Glenner. 1983. Scrapie prions aggregate to form amyloid-like birefringent rods. Cell. 35:349-358.
51. Prusiner, S. B., M. R. Scott, S. J. DeArmond, and F. E. Cohen. 1998. Prion protein biology. Cell. 93:337-348.
52. Ragg, E., F. Tagliavini, P. Malesani, L. Monticelli, O. Bugiani, G. Forloni, and M. Salmona. 1999. Determination of solution conformations of PrP106-126, a neurotoxic fragment of prion protein, by IH NMR and restrained molecular dynamics. Eur. J. Biochem. 266:1192-1201.
53. Rapoport, T. A. 1985. Protein translocation across and integration into membranes. Crit. Rev. Biochem. 20:73-137.
54. Selvaggini, C., L. De Gioia, L. Cantu, E. Ghibaudi, L. Diomede, F. Passerini, G. Forloni, O. Bugiani, F. Tagliavini, and M. Salmona. 1993. Molecular characteristics of a protease-resistant, amyloidogenic and neurotoxic peptide homologous to residues 106-126 of the prion protein. Biochem. Biophys. Res. Commun. 194:1380-1386.
55. Sitaram, N., and R. Nagaraj. 1993. Interaction of the 47-residue anti-bacterial peptide seminalplasmin and its 13-residue fragment which has antibacterial and hemolytic activities with model membranes. Biochemistry. 32:3124-3130.
56. Sreerama, N., S. Y. Venyaminov, and R. W. Woody. 2000. Estimation of protein secondary structure from circular dichroism spectra: inclusion of denatured proteins with native proteins in the analysis. Anal. Biol. 287:243-251.
57. Stewart, J. M., and J. D. Young. 1984. Solid Phase Peptide Synthesis. Pierce Chemical Company, Rockford, Il.
58. Storrs, R. W., D. Truckses, and D. E. Wemmer. 1992. Helix propagation in trifluoroethanol solutions. Biopolymers. 32:1695-1702.
59. Tagliavini, F., F. Prelli, J. Ghiso, O. Bugiani, D. Serban, S. B. Prusiner, M. R. Farlow, B. Ghetti, and B. Frangiono. 1991. Amyloid protein of Gerstmann-Sträussler-Scheinker disease (Indiana kindred) is an 11 kd fragment of prion protein with an N-terminal glycine at codon 58. EMBO J. 10:513-519.
60. Tagliavini, F., F. Prelli, L. Verga, G. Giaccone, R. Sarma, P. Gorevic, B. Ghetti, F. Passerini, E. Ghibaudi, G. Forloni, M. Salmona, O. Bugiani, and B. Fragioni. 1993. Synthetic peptides homologous to prion protein residues 106-147 form amyloid-like fibrils in vitro. Proc. Natl. Acad. Sci. USA. 90:9678-9682.
61. Tagliavini, F., F. Prelli, M. Porro, G. Rossi, G. Giaccone, M. R. Farlow, S. R. Dlouhy, B. Ghetti, O. Bugiani, and B. Frangione. 1994. Amyloid fibrils in Gerstmann-Straussler-Scheinker disease (Indiana and Swedish kindreds) express only PrP peptides encoded by the mutant allele. Cell. 79:695-703.
62. Wickner, W. T., and H. F. Lodish. 1985. Multiple mechanisms of protein insertion into and across membranes. Science. 230:400-407.
63. Wille, H., M. D. Michelitsch, V. Guenebaut, S. Supattapone, A. Serban, F. E. Cohen, D. A. Agard, and S. B. Prusiner. 2002. Structural studies of the scrapie prion protein by electron crystallography. Proc. Natl. Acad. Sci. USA. 99:3563-3568.
64. Williams, R. C. 1977. Use of polylysine for adsorption of nuclei acids and enzymes to electron microscope specimen films. Proc. Natl. Acad. Sci. USA. 74:2311-2315.
65. Wilson, J. C., K. J. Nielson, M. J. McLeish, and D. J. Craik. 1994. A determination of the solution conformation of the nonmammalian Tachykinin eledoisin by NMR and CD spectroscopy. Biochemistry. 33:6802-6811.
66. Xu, X., L. G. Cooper, P. J. DiMario, and J. W. Nelson. 1995. Helix formation in model peptides based on nucleolin TPAKK motifs. Biopolymers. 35:93-102.
67. Zhang, M., and H. J. Vogel. 1994. The calmodulin-binding domain of caldesmon binds to calmodulin in an alpha-helical conformation. Biochemistry. 33:1163-1171.
68. Zhou, N. E., C. M. Kay, B. D. Sykes, and R. S. Hodges. 1993. A single-stranded amphipathic alpha-helix in aqueous solution: design, structural characterization, and its application for determining alpha-helical propensities of amino acids. Biochemistry. 32:6190-6197.