An improved method of preparing the amyloid β-protein for fibrillogenesis and neurotoxicity experiments

References

• Sipe J D. Amyloidosis. Ann Rev Biochem 1992; 61: 947–975
   PubMed Web of Science ®Google Scholar
• Selkoe D J. The molecular pathology of Alzheimer's disease. Neuron 1991; 6: 487–498
   PubMed Web of Science ®Google Scholar
• Selkoe D J. Translating cell biology into therapeutic advances in Alzheimer's disease. Nature 1999; 399: A23–A31
   PubMed Web of Science ®Google Scholar
• Glenner G G. Amyloid deposits and amyloidosis. The β-fibrilloses (First of two parts). New Eng J Med 1980; 302: 1283–1292
   PubMed Web of Science ®Google Scholar
• Glenner G G. Amyloid deposits and amyloidosis: The β-fibrilloses (Second of two parts). New Eng J Med 1980; 302: 1333–1343
   PubMed Web of Science ®Google Scholar
• Kirschner D A, Abraham C, Selkoe D J. X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer's disease indicates cross-β conformation. Proc Natl Acad Sci USA 1986; 83: 503–507
   PubMed Web of Science ®Google Scholar
• Yankner B A, Duffy L K, Kirschner D A. Neurotrophic and neurotoxic effects of amyloid β protein: reversal by tachykinin neuropeptides. Science 1990; 250: 279–282
   PubMed Web of Science ®Google Scholar
• Pike C J, Burdick D, Walencewicz A J, Glabe C G, Cotman C W. Neurodegeneration induced by β-amyloid peptides in vitro: The role of peptide assembly state. J Neurosci 1993; 13: 1676–1687
   PubMed Web of Science ®Google Scholar
• Pike C J, Walencewicz A J, Glabe C G, Cotman C W. In vitro aging of β-amyloid protein causes peptide aggregation and neurotoxicity. Brain Res 1991; 563: 311–314
   PubMed Web of Science ®Google Scholar
• Lambert M P, Barlow A K, Chromy B A, Edwards C, Freed R, Liosatos M, Morgan T E, Rozovsky I, Trommer B, Viola K L, Wals P, Zhang C, Finch C E, Krafft G A, Klein W L. Diffusible, nonfibrillar ligands derived from Aβ1-42 are potent central nervous system neurotoxins. Proc Natl Acad Sci USA 1998; 95: 6448–6453
   PubMed Web of Science ®Google Scholar
• Walsh D M, Hartley D M, Kusumoto Y, Fezoui Y, Condron M M, Lomakin A, Benedek G B, Selkoe D J, Teplow D B. Amyloid β-protein fibrillogenesis - Structure and biological activity of protofibrillar intermediates. J Biol Chem 1999; 274: 25945–25952
   PubMed Web of Science ®Google Scholar
• Hartley D M, Walsh D M, Ye C P, Diehl T S, Vassilev P M, Teplow D B, Selkoe D J. The relative neurotoxicity of discrete forms of Aβ observed during fibrillogenesis. J Neurosci 1999; 19: 8876–8884
   PubMed Web of Science ®Google Scholar
• Simmons L K, May P C, Tomaselli K J, Rydel R E, Fuson K S, Brigham E F, Wright S, Lieberburg I, Becker G W, Brems D N, Li W Y. Secondary structure of amyloid β peptide correlates with neurotoxic activity in vitro. Molecular Pharm 1994; 45: 373–379
   PubMed Web of Science ®Google Scholar
• Howlett D R, Jennings K H, Lee D C, Clark M S, Brown F, Wetzel R, Wood S J, Camilleri P, Roberts G W. Aggregation state and neurotoxic properties of Alzheimer β-amyloid peptide. Neurodegeneration 1995; 4: 23–32
   PubMedGoogle Scholar
• Soto C, Castano E M, Kumar R A, Beavis R C, Frangione B. Fibrillogenesis of synthetic amyloid-β peptides is dependent on their initial secondary structure. Neurosci Lett 1995; 200: 105–108
   PubMed Web of Science ®Google Scholar
• Jao S C, Ma K, Talafous J, Orlando R, Zagorski M G. Trifluoroacetic acid pretreatment reproducibly disaggregates the amyloid β-peptide. Amyloid: Int J Exp Clin Invest 1997; 4: 240–252
   Web of Science ®Google Scholar
• Wood S J, Maleeff B, Hart T, Wetzel R. Physical, morphological and functional differences between pH 5. 8 and 7. 4 aggregates of the Alzheimer's amyloid peptide Aβ. J Mol Biol 1996; 256: 870–877
   PubMed Web of Science ®Google Scholar
• Snyder S W, Ladror U S, Wade W S, Wang G T, Barrett L W, Matayoshi E D, Huffaker H J, Krafft G A, Holzman T F. Amyloid-β aggregation: selective inhibition of aggregation in mixtures of amyloid with different chain lengths. Biophysical J 1994; 67: 1216–1228
   PubMed Web of Science ®Google Scholar
• Shen C L, Murphy R M. Solvent effects on self-assembly of β-amyloid peptide. Biophysical J 1995; 69: 640–651
   PubMed Web of Science ®Google Scholar
• Barrow C J, Yasuda A, Kenny P TM, Zagorski M. Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer's disease. J Mol Biol 1992; 225: 1075–1093
   PubMed Web of Science ®Google Scholar
• Kaneko I. Conformations of β-amyloid in solution -Reply. J Neurochem 1997; 68: 438–439
   Web of Science ®Google Scholar
• Walsh D M, Lomakin A, Benedek G B, Condron M M, Teplow D B. Amyloid β-protein fibrillogenesis - Detection of a protofibrillar intermediate. J Biol Chem 1997; 272: 22364–22372
   PubMed Web of Science ®Google Scholar
• Perczel A, Park K, Fasman G D. Analysis of the circular dichroism spectrum of proteins using the Convex Constraint Algorithm: A practical guide. Anal Biochem 1992; 203: 83–93
   PubMed Web of Science ®Google Scholar
• Brahms S, Brahms J. Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism. J Mol Biol 1980; 138: 149–178
   PubMed Web of Science ®Google Scholar
• Klunk W E, Pettegrew J W, Abraham D J. Quantitative evaluation of congo red binding to amyloid-like proteins with a β-pleated sheet conformation. J Histochem Cytochem 1989; 37: 1273–1281
   PubMed Web of Science ®Google Scholar
• Ding T T, Harper J D. Analysis of amyloid-β assemblies using tapping mode atomic force microscopy under ambient conditions. Amyloid, Prions, and Other Protein Aggregates. Methods in Enzymology, R. Wetzel. Academic Press, San Diego 1999; 309: 510–525
   Google Scholar
• Hartley D M, Kurth M C, Bjerkness L, Weiss J H, Choi D W. Glutamate receptor-induced 45Ca2+ accumulation in cortical cell culture correlates with subsequent neuronal degeneration. J Neurosci 1993; 13: 1993–2000
   PubMed Web of Science ®Google Scholar
• Seshadri S, Khurana R, Fink A L. Fourier transform infrared spectroscopy in analysis of protein deposits. Amyloid, Prions, and Other Protein Aggregates. Methods in Enzymology, R. Wetzel. Academic Press, San Diego 1999; 309: 559–576
   Google Scholar
• Jackson M, Mantsch H H. The use and misuse of FTIR spectroscopy in the determination of protein structure. Crit Rev Biochem Mol Biol 1995; 30: 95–120
   PubMed Web of Science ®Google Scholar
• Lee J P, Stimson E R, Ghilardi J R, Mantyh P W, Lu Y A, Felix A M, Llanos W, Behbin A, Cummings M, Vancriekinge M, Timms W, Maggio J E. 1H NMR of Aβ amyloid peptide congeners in water solution. Conformational changes correlate with plaque competence. Biochemistry 1995; 34: 5191–5200
   PubMed Web of Science ®Google Scholar
• Harper J D, Wong S S, Lieber C M, Lansbury P T. Observation of metastable Aβ amyloid protofibrils by atomic force microscopy. Chem Biol 1997; 4: 119–125
   PubMed Web of Science ®Google Scholar
• Richardson J S, Richardson D C. Principles and patterns of protein conformation. Prediction of protein structures and the principles of protein conformation, G. D. Fasman. Plenum Press, New York, NY 1989; 1–98
   Google Scholar
• Soto C, Castano E M, Frangione B, Inestrosa N C. The a-helical to P-strand transition in die amino-terminal fragment of the amyloid β-peptide modulates amyloid formation. J Biol Chem 1995; 270: 3063–3067
   PubMed Web of Science ®Google Scholar
• Nybo M, Svehag S E, Nielsen E H. An ultrastruc-tural study of amyloid intermediates in Aβ1-42 fibrillogenesis. Scand J Immunol 1999; 49: 219–223
   PubMed Web of Science ®Google Scholar