Design of metastable β-sheet oligomers from natively unstructured peptide

ACS Chemical Neuroscience

Volumn 4, Issue 12, 2013, Pages 1520-1523

  Guerrero Muñoz, Marcos J ^a   Castillo Carranza, Diana L ^a   Sengupta, Urmi ^a   White, Mark A ^a   Kayed, Rakez ^a  

^a University of Texas Medical Branch School of Medicine   (United States)

Author keywords

Amyloid oligomer; constrained peptide; prion

Indexed keywords

AMYLOID; EPITOPE; GLYCINE; METHIONINE; OLIGOMER; PRION PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; BETA SHEET; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; GEL PERMEATION CHROMATOGRAPHY; MOLECULAR WEIGHT; PRIORITY JOURNAL; PROTEIN STABILITY;

AMINO ACID SEQUENCE; AMYLOIDOGENIC PROTEINS; BIOMIMETICS; HUMANS; MOLECULAR SEQUENCE DATA; PEPTIDES; PRIONS; PROTEIN STRUCTURE, SECONDARY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

EID: 84890592774     PISSN: None     EISSN: 19487193     Source Type: Journal    
DOI: 10.1021/cn4001395     Document Type: Article

References (31)

1. Terry, R. D. (1996) The pathogenesis of Alzheimer disease: an alternative to the amyloid hypothesis J. Neuropathol. Exp. Neurol. 55, 1023-1025
2. Crystal, H., Dickson, D., Fuld, P., Masur, D., Scott, R., Mehler, M., Masdeu, J., Kawas, C., Aronson, M., and Wolfson, L. (1988) Clinico-pathologic studies in dementia: nondemented subjects with pathologically confirmed Alzheimer's disease Neurology 38, 1682-1687
3. Davies, L., Wolska, B., Hilbich, C., Multhaup, G., Martins, R., Simms, G., Beyreuther, K., and Masters, C. L. (1988) A4 amyloid protein deposition and the diagnosis of Alzheimer's disease: prevalence in aged brains determined by immunocytochemistry compared with conventional neuropathologic techniques Neurology 38, 1688-1693
4. Price, J. L. and Morris, J. C. (1999) Tangles and plaques in nondemented aging and ″preclinical″ Alzheimer's disease Ann. Neurol. 45, 358-368
5. Billings, L. M., Oddo, S., Green, K. N., McGaugh, J. L., and Laferla, F. M. (2005) Intraneuronal Abeta causes the onset of early Alzheimer's disease-related cognitive deficits in transgenic mice Neuron 45, 675-688
6. Westerman, M. A., Cooper-Blacketer, D., Mariash, A., Kotilinek, L., Kawarabayashi, T., Younkin, L. H., Carlson, G. A., Younkin, S. G., and Ashe, K. H. (2002) The relationship between Abeta and memory in the Tg2576 mouse model of Alzheimer's disease J. Neurosci. 22, 1858-1867
7. McLean, C. A., Cherny, R. A., Fraser, F. W., Fuller, S. J., Smith, M. J., Beyreuther, K., Bush, A. I., and Masters, C. L. (1999) Soluble pool of Abeta amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease Ann. Neurol. 46, 860-866
8. Lue, L. F., Kuo, Y. M., Roher, A. E., Brachova, L., Shen, Y., Sue, L., Beach, T., Kurth, J. H., Rydel, R. E., and Rogers, J. (1999) Soluble amyloid beta peptide concentration as a predictor of synaptic change in Alzheimer's disease Am. J. Pathol. 155, 853-862
9. Haass, C. and Selkoe, D. J. (2007) Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide Nat. Rev. Mol. Cell Biol. 8, 101-112
10. Kayed, R., Head, E., Sarsoza, F., Saing, T., Cotman, C. W., Necula, M., Margol, L., Wu, J., Breydo, L., Thompson, J. L., Rasool, S., Gurlo, T., Butler, P., and Glabe, C. G. (2007) Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers Mol. Neurodegener. 2, 18
11. Kayed, R., Pensalfini, A., Margol, L., Sokolov, Y., Sarsoza, F., Head, E., Hall, J., and Glabe, C. (2009) Annular protofibrils are a structurally and functionally distinct type of amyloid oligomer J. Biol. Chem. 284, 4230-4237
12. Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., and Glabe, C. G. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis Science 300, 486-489
13. Wu, J. W., Breydo, L., Isas, J. M., Lee, J., Kuznetsov, Y. G., Langen, R., and Glabe, C. (2010) Fibrillar Oligomers Nucleate the Oligomerization of Monomeric Amyloid {beta} but Do Not Seed Fibril Formation J. Biol. Chem. 285, 6071-6079
14. Butterfield, S. M. and Lashuel, H. A. (2010) Amyloidogenic protein-membrane interactions: mechanistic insight from model systems Angew. Chem., Int. Ed. Engl. 49, 5628-5654
15. Andreetto, E., Yan, L. M., Tatarek-Nossol, M., Velkova, A., Frank, R., and Kapurniotu, A. (2010) Identification of hot regions of the Aβ-IAPP interaction interface as high-affinity binding sites in both cross- and self-association Angew. Chem., Int. Ed. Engl. 49, 3081-3085
16. Yoon, S., Welsh, W. J., Jung, H., and Yoo, Y. D. (2007) CSSP2: an improved method for predicting contact-dependent secondary structure propensity Comput. Biol. Chem. 31, 373-377
17. Larkin, M. A., Blackshields, G., Brown, N. P., Chenna, R., McGettigan, P. A., McWilliam, H., Valentin, F., Wallace, I. M., Wilm, A., Lopez, R., Thompson, J. D., Gibson, T. J., and Higgins, D. G. (2007) Clustal W and Clustal X version 2.0 Bioinformatics 23, 2947-2948
18. Groenning, M. (2010) Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils-current status J. Chem. Biol. 3, 1-18
19. Hawe, A., Sutter, M., and Jiskoot, W. (2008) Extrinsic fluorescent dyes as tools for protein characterization Pharm. Res. 25, 1487-1499
20. Jackson, M. and Mantsch, H. H. (1995) The use and misuse of FTIR spectroscopy in the determination of protein structure Crit. Rev. Biochem. Mol. Biol. 30, 95-120
21. Prangkio, P., Yusko, E. C., Sept, D., Yang, J., and Mayer, M. (2012) Multivariate analyses of amyloid-beta oligomer populations indicate a connection between pore formation and cytotoxicity PLoS One 7, e47261
22. Philo, J. S. (2006) Is any measurement method optimal for all aggregate sizes and types? AAPS J. 8, E564-571
23. Harper, J. D., Wong, S. S., Lieber, C. M., and Lansbury, P. T., Jr. (1999) Assembly of A beta amyloid protofibrils: an in vitro model for a possible early event in Alzheimer's disease Biochemistry 38, 8972-8980
24. Peretz, D., Williamson, R. A., Matsunaga, Y., Serban, H., Pinilla, C., Bastidas, R. B., Rozenshteyn, R., James, T. L., Houghten, R. A., Cohen, F. E., Prusiner, S. B., and Burton, D. R. (1997) A conformational transition at the N terminus of the prion protein features in formation of the scrapie isoform J. Mol. Biol. 273, 614-622
25. Gasset, M., Baldwin, M. A., Lloyd, D. H., Gabriel, J. M., Holtzman, D. M., Cohen, F., Fletterick, R., and Prusiner, S. B. (1992) Predicted alpha-helical regions of the prion protein when synthesized as peptides form amyloid Proc. Natl. Acad. Sci. U.S.A. 89, 10940-10944
26. Tagliavini, F., Prelli, F., Verga, L., Giaccone, G., Sarma, R., Gorevic, P., Ghetti, B., Passerini, F., Ghibaudi, E., and Forloni, G. 1993, Synthetic peptides homologous to prion protein residues 106-147 form amyloid-like fibrils in vitro Proc. Natl. Acad. Sci. U.S.A. 90, 9678-9682
27. Salmona, M., Morbin, M., Massignan, T., Colombo, L., Mazzoleni, G., Capobianco, R., Diomede, L., Thaler, F., Mollica, L., Musco, G., Kourie, J. J., Bugiani, O., Sharma, D., Inouye, H., Kirschner, D. A., Forloni, G., and Tagliavini, F. (2003) Structural properties of Gerstmann-Straussler-Scheinker disease amyloid protein J. Biol. Chem. 278, 48146-48153
28. Thaa, B., Zahn, R., Matthey, U., Kroneck, P. M., Burkle, A., and Fritz, G. (2008) The deletion of amino acids 114-121 in the TM1 domain of mouse prion protein stabilizes its conformation but does not affect the overall structure Biochim. Biophys. Acta 1783, 1076-1084
29. Holscher, C., Delius, H., and Burkle, A. (1998) Overexpression of nonconvertible PrPc delta114-121 in scrapie-infected mouse neuroblastoma cells leads to trans-dominant inhibition of wild-type PrP(Sc) accumulation J. Virol. 72, 1153-1159
30. Norstrom, E. M. and Mastrianni, J. A. (2005) The AGAAAAGA palindrome in PrP is required to generate a productive PrPSc-PrPC complex that leads to prion propagation J. Biol. Chem. 280, 27236-27243
31. Simoneau, S., Rezaei, H., Sales, N., Kaiser-Schulz, G., Lefebvre-Roque, M., Vidal, C., Fournier, J. G., Comte, J., Wopfner, F., Grosclaude, J., Schatzl, H., and Lasmezas, C. I. (2007) In vitro and in vivo neurotoxicity of prion protein oligomers PLoS Pathog. 3, e125