Correlations among morphology, β-sheet stability, and molecular structure in prion peptide aggregates

Biochemistry

Volumn 44, Issue 12, 2005, Pages 4720-4726

  Petty, Sarah A ^a   Adalsteinsson, Thorsteinn ^a   Decatur, Sean M ^a  

^a MOUNT HOLYOKE COLLEGE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ATOMIC FORCE MICROSCOPY; DISEASES; MOLECULAR STRUCTURE; SUBSTITUTION REACTIONS; THERMODYNAMIC STABILITY;

FIBROUS NETWORKS; PEPTIDES; PROTOFIBRILS; SHEET AGGREGATES;

PROTEINS;

PRION PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; ATOMIC FORCE MICROSCOPY; BETA SHEET; CORRELATION ANALYSIS; FIBER; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; THERMOSTABILITY;

ALANINE; AMINO ACID SUBSTITUTION; ANIMALS; CARBON ISOTOPES; CRICETINAE; MESOCRICETUS; MICROSCOPY, ATOMIC FORCE; PEPTIDE FRAGMENTS; PRIONS; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ALIGNMENT; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; THERMODYNAMICS;

EID: 15444367176     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047445a     Document Type: Article

References (25)

1. Dobson, C. M. (2003) Protein-misfolding diseases: Getting out of shape, Nature 426, 884-890.
2. Prusiner, S. B. (1991) Molecular biology of prion diseases, Science 252, 1515-1522.
3. Scherzinger, E., Lurz, R., Turmaine, M., Mangiarini, L., Hollenbach, B., Hasenbank, R., Bates, G. P., Davies, S. W., Lehrach, H., and Wanker, E. E. (1997) Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo, Cell 90, 549-558.
4. Fandrich, M., Fletcher, M. A., and Dobson, C. M. (2001) Amyloid fibrils from muscle myoglobin, Nature 410, 165-166.
5. Walsh, D. M., Hartley, D. M., Kusumoto, Y., Fezoui, Y., Condron, M. M., Lomakin, A., Benedek, G. B., Selkoe, D. J., and Teplow, D. B. (1999) Amyloid β-protein fibrillogenesis, J. Biol. Chem. 274, 25945-25952.
6. Serpell, L. C., Blake, C. C. F., and Fraser, P. E. (2000) Molecular structure of a fibrillar Alzheimer's aβ fragment, Biochemistry 39, 13269-13275.
7. Goldsbury, C., Kistler, J., Aebi, U., Arvinte, T., and Cooper, G. J. S. (1999) Watching amyloid fibrils grow by time-lapse atomic force microscopy, J. Mol. Biol. 285, 33-39.
8. Huang, T. H. J. Yang, D-S., Fraser, P. E., and Chakrabartty, A. (2000) Alternate aggregation pathways of the Alzheimer β-amyloid peptide. An in vitro model of preamyloid, J. Biol. Chem. 275, 36436-36440.
9. Harper, J. D., Wong, S. S., Lieber, C. M., and Lansbury, P. T. (1997) Atomic force microscopic images of seeding fibril formation and fibril branching by the Alzheimer's disease amyloid-β protein, Chem. Biol. 4, 419-425.
10. Makin, O. S., and Serpell, L. C. (2004) Structural characterisation of islet amyloid polypeptide fibrils, J. Mol. Biol. 335, 1279-1288.
11. Serpell, L. C., and Smith, J. M. (2000) Direct visualisation of the β-sheet structure of synthetic Alzheimer's amyloid, J. Mol. Biol. 299, 225-231.
12. Gasset, M., Baldwin, M. A., Lloyd, D. H., Gabriel, J.-M., Holtzman, D. M., Cohen, F. E., Fletterick, R., and Prusiner, S. B. (1992) Predicted α-helical regions of the prion protein when synthesized as peptides form amyloid, Proc. Natl. Acad. Sci. U.S.A. 89, 10940-10944.
13. Nguyen, J., Baldwin, M. A., Cohen, F. E., and Prusiner, S. B. (1995) Prion protein peptides induce α-helix to β-sheet conformational transitions, Biochemistry 34, 4186-4192.
14. Conway, K. A., Harper, J. D., and Lansbury, P. T. (2000) Fibrils formed in vitro from α-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid, Biochemistry 39, 2552-2563.
15. Halverson, K., Sucholeiki, I., Ashbury, T. T.,and Lansbury, P. T. (1991) Location of β-sheet-forming sequences in amyloid proteins by FTIR, J. Am. Chem. Soc. 113, 6701-6703.
16. Laws, D. D., Bitter, H.-M., Liu, K., Ball, H. L., Kaneko, K., Wille, H., Cohen, F. E., Prusiner, S. B., Pines, A., and Wemmer, D. E. (2001) Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration, Proc. Natl. Acad. Sci. U.S.A. 98, 11686-11690.
17. Brown, D. R. (2000) Altered toxicity of the prion protein peptide PrP(106-126) carrying the alal 17 → val mutation, Biochem. J. 346, 785-791.
18. Silva, R. A. G. D., Barber-Armstrong, W., and Decatur, S. M. (2003) The organization and assembly of a β-sheet formed by a prion peptide in solution: an isotope-edited FTIR study, J. Am. Chem. Soc. 125, 13674-13675.
19. Chirgadze, Y. N., Shestopalov, B. V., and Venyaminov, S. Y. (1973) Intensities and other spectral parameters of infrared amide bands of polypeptides in the β- and random forms, Biopolymers 12, 1337-1351.
20. 13C isotope labeling of hydrophobic peptides. origin of the anomalous intensity distribution in the infrared amide I spectral region of β-sheet structures, J. Am. Chem. Soc. 122, 677-683.
21. Kubelka, J., and Keiderling, T. A. (2001) The anomalous infrared amide I intensity distribution in 13c isotopically labeled peptide β-sheets comes from Extended Multiple-Stranded Structures. An ab initio study, J. Am. Chem. Soc. 123, 6142-6150.
22. Muller, D. J., and Engel, A. (1997) The height of biomolecules measured with the atomic force microscope depends on electrostatic interactions, Biophys. J. 73, 1663-1644.
23. Kubelka, J., and Keiderling, T. A. (2001) Differentiation of β-sheet-forming structures: Ab initio-based simulations of IR absorption and vibrational CD for model peptide and protein β-sheets, J. Am. Chem. Soc. 123, 12048-12058.
24. Doig, A. J., and Sternberg, M. J. E. (1995) Side-chain conformational entropy in protein folding, Protein Sci. 4, 2247-2251.
25. Creamer, T. P. and Rose, G. D. (1992) Side-chain entropy opposes α-helix formation but rationalizes experimentally determined helix-forming propensities, Proc. Natl. Acad. Sci. U.S.A. 89, 5937-5941.