Histidine residues underlie Congo red binding to Aβ analogs

References

• Klunk W E, Pettegrew J W, Abraham D J. Two simple methods for quantifying low-affinity dye-substrate binding. J Histochem Cytochem 1989; 37: 1293–1297
   PubMed Web of Science ®Google Scholar
• Klunk W E, Debnath M L, Pettegrew J W. Development of small molecule probes for the β-amyloid protein of Alzheimer's disease. Neumbiol Aging 1994; 15: 691–698
   PubMed Web of Science ®Google Scholar
• Burke M J, Rougvie M A. Cross-beta protein structures. I. Insulin Fibrils. Biochemistry 1972; 11: 2435–2439
   PubMed Web of Science ®Google Scholar
• Brange J, Dodson G G, Edwards D J, Holden P H, Whittingham J L. A model of insulin fibrils derived from the x-ray crystal structure of a monomeric insulin (despentapeptideinsulian). Proteins: Structure, Function, and Genetics 1997; 27: 507–516
   PubMed Web of Science ®Google Scholar
• Koltun W L, Waugh D F, Bear R S. An x-ray diffraction investigation of selected types of insulin fibrils. J Amer Chem Soc 1954; 76: 413–417
   Web of Science ®Google Scholar
• Burdick D, Soreghan B, Kwon M, Kosmoski J, Knauer M, Henschen A, Yates J, Cotman C, Glabe C. Assembly and aggregation properties of synthetic Alzheimer's A4/ β amyloid peptide analogs. J Biol Chem 1992; 267: 546–554
   PubMed 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
• Kirschner D A, Inouye H, Duffy L K, Sinclair A, Lind M, Selkoe D J. Synthetic β-protein of Alzheimer disease forms amyloid-like fibrils in vitro. Proc Natl Acad Sci USA 1987; 84: 6953–6957
   PubMed Web of Science ®Google Scholar
• Masters C L, Multhaup G, Simms G, Pottgiesser J, Martins R N, Beyreuther K. Neuronal origin of a cerebral amyloid: neurofibrillary tangles of Alzheimer's disease contain the same protein as the amyloid of plaque cores and blood vessels. EMBO (EurMol Biol Organ) J 1985; 4: 2757–2763
   PubMed Web of Science ®Google Scholar
• Fraser P E, Nguyen J T, Chin D T, Kirschner D A. Effects of sulfate ions on Alzheimer β/A4 peptide assemblies: Implications for amyloid fibril-proteoglycan interactions. J Neurochem 1992; 59: 1531–1540
   PubMed Web of Science ®Google Scholar
• Inouye H, Fraser P E, Kirschner D A. Structure of β-crystallite assemblies formed by Alzheimer β-amyloid protein analogs: Analysis by x-ray diffraction. Biophys J 1993; 64: 502–519
   PubMed Web of Science ®Google Scholar
• Fraser P E, McLachlan D R, Surewicz W K, Mizzen C A, Snow A D, Nguyen J T, Kirschner D A. Conformation and fibrillogenesis of Alzheimer Aβ peptides with selected substitution of charged residues. J Mol Biol 1994; 244: 64–73
   PubMed Web of Science ®Google Scholar
• Barrow C J, Yasuda A, Kenny P TM, Zagorski M G. 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
• Puchtler H, Sweat F, Levine M. On the binding of Congo Red by amyloid. J Histochem Cytochem 1962; 10: 355–364
   Web of Science ®Google Scholar
• Fraser P E, Nguyen J T, Inouye H, Surewicz W K, Selkoe D J, Podlisny M B, Kirschner D A. Fibril formation by primate, rodent and Dutch-Hemorrhagic analogs of Alzheimer amyloid β-protein. Biochemistry 1992; 31: 10716–10723
   PubMed Web of Science ®Google Scholar
• Giordano T, Pan J B, Monteggia L M, Holzman T F, Snyder S W, Krafft G, Ghanbari H, Kowall N W. Similarities between beta amyloid peptides 1-40 and 40-1: Effects on aggregation, toxicity in vitro, and injection in young and aged rats. Exp Neurol 1994; 125: 175–182
   PubMed Web of Science ®Google Scholar
• Edwards R A, Woody R W. Spectroscopic studies of Cibacron Blue and Congo Red bound to dehydrogenases and kinases. Evaluation of dyes as probes of the dinucleotide fold. Biochemistry 1979; 18: 5197–5204
   PubMed Web of Science ®Google Scholar
• Gutbezahl B, Grunwald E. The effect of solvent on equilibrium and rate constants. II. The measurement and correlation of acid dissociation constants of anilinium and ammonium salts in the system ethanol-water. J Amer Chem Soc 1953; 75: 559–574
   Web of Science ®Google Scholar
• Bates R G. Determination of pH. Theory and Practice. John Wiley & Sons, Inc, New York 1973
   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
• Inouye H, Kirschner D A. Membrane interactions in nerve myelin: II Determination of surface charge from biochemical data. Biophys J 1988; 53: 247–260
   PubMed Web of Science ®Google Scholar
• Tanford C, Roxby R. Interpretation of protein titration curves. Application to lysozyme. Biochemistry 1972; 11: 2192–2198
   PubMed Web of Science ®Google Scholar
• Nozaki Y, Tanford C. Examination of titration behavior. Meth Enzymol 1967; 11: 715–734
   Google Scholar
• Cantor C R, Schimmel P R. Biophysical Chemistry. WH Freeman and Company, San Francisco 1980
   Google Scholar
• Tanford C. Physical Chemistry of Macromolecules. John Wiley & Sons, Inc, New York 1961
   Google Scholar
• Scatchard G. The attractions of proteins for small molecules and ions. Ann NY Acad Sci 1949; 51: 660–672
   Web of Science ®Google Scholar
• Mera S L, Davies J D. Differential Congo Red staining: the effects of pH, non-aqueous solvents and the substrate. Histochem J 1984; 16: 195–210
   PubMedGoogle Scholar
• Miyakawa T, Watanabe K, Katsuragi S. infrastructure of amyloid fibrils in Alzheimer's disease and Down's syndrome. Virchows Arch [Cell Pathol] 1986; 52: 99–106
   Google Scholar
• Miyakawa T, Katsuragi S, Kuramoto R. Ultrastructure of perivascular amyloid fibrils in Alzheimer's disease. Virchows Arch [Cell Pathol] 1988; 56: 21–24
   Google Scholar
• Fraser P E, Duffy L K, O'Malley M B, Nguyen J, Inouye H, Kirschner D A. Morphology and antibody recognition of synthetic β-amyloid peptides. J Neurosci Res 1991; 28: 474–485
   PubMed Web of Science ®Google Scholar
• Fraser P E, Nguyen J, Surewicz W K, Kirschner D A. pH-dependent structural transitions of Alzheimer amyloid peptides. Biophys J 1991; 60: 1190–1201
   PubMed Web of Science ®Google Scholar
• Malinchik S B, Inouye H, Szumowski K E, Kirschner D A. Structural analysis of Alzheimer's β(1-40). amyloid: Protofilament assembly of tubular fibrils. Biophys J 1998; 74: 537–545
   PubMed Web of Science ®Google Scholar
• Inouye H, Kirschner D A. Refined fibril structures: The hydrophobic core in Alzheimer's β-amyloid and prion as revealed by X-ray diffraction. The Nature and Origin of Amyloid Fibrils, G R Bock, J A Goode. Ciba Foundation Symposium No. 199, John Wiley & Sons, Chichester, UK and New York, NY 1996; 22–39
   Google Scholar
• Watson D J, Lander A D, Selkoe D J. Heparin-bind-ing properties of the amyloidogenic peptides Aβ and amylin. J Biol Chem 1997; 272: 31617–31624
   PubMed Web of Science ®Google Scholar
• Kisilevsky R. Theme and variations on a string of amyloid. Neurobiol Aging 1989; 10: 499–500
   PubMed Web of Science ®Google Scholar
• Brunden K R, Richter-Cook N J, Chaturvedi N, Frederickson R CA. pH-dependent binding of synthetic β-amyloid peptides to glycosaminoglycans. J Neurochem 1993; 61: 2147–2154
   PubMed Web of Science ®Google Scholar
• Huang T HJ, Fraser P E, Chakrabartty A. Fibrillogenesis of Alzheimer Aβ peptides studies by fluorescence energy transfer. J Mol Biol 1997; 269: 214–224
   PubMed Web of Science ®Google Scholar
• Joshi M D, Hedberg A, McIntosh L P. Complete measurement of the pKa values of the carboxyl and imidazole groups in Bacillus circulans xylanase. Protein Sci 1997; 6: 2667–2670
   PubMed Web of Science ®Google Scholar
• Ashburn T T, Han H, McGuinness B F, Lansbury P T, Jr. Amyloid probes based on Congo Red distinguish between fibrils comprising different peptides. Chem Bio 1996; 3: 351–358
   PubMedGoogle Scholar
• LeVine H, III. Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution. Protein Sci 1993; 2: 404–410
   PubMed Web of Science ®Google Scholar
• Bush A I, Pettingell W H, Multhaup G, Paradis M D, Vonsattel J-P, Gusella J F, Beyreuther K, Masters C L, Tanzi R E. Rapid induction of Alzheimer Aβ amyloid formation by zinc. Science 1994; 265: 1464–1467
   PubMed Web of Science ®Google Scholar
• Tjernberg L O, Näslund J, Lindqvist F, Johansson J, Karlström A R, Thyberg J, Terenius L, Nordstedt C. Arrest of β-amyloid fibril formation by a pentapeptide ligand. J Biol Chem 1996; 271: 8545–8548
   PubMed Web of Science ®Google Scholar
• Soto C, Sigurdsson E M, Morelli L, Kumar R A, Castaño E M, Frangione B. βP-sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: Implications for Alzheimer's therapy. Nature Med 1998; 4: 822–826
   PubMed Web of Science ®Google Scholar
• Kisilevsky R, Fraser P E. Aβ amyloidogenesis: Unique, or variation on a systemic theme?. Crit Rev Biochem Mol Biol 1997; 32: 361–404
   PubMed Web of Science ®Google Scholar
• Schwarzman A L, Gregori L, Vitek M P, Lyubski S, Strittmatter W J, Enghilde J J, Bhasin R, Silverman J, Weisgraber K H, et al. Transthyretin sequesters amyloid β-protein and prevents amyloid formation. Proc Natl Acad Sci USA 1994; 91: 8368–8372
   PubMed Web of Science ®Google Scholar
• Fraser P E, Nguyen J T, McLachlan D R, Abraham C R, Kirschner D A. αl-Antichymotrypsin binding to Alzheimer Aβ peptides is sequence specific and induces fibril disaggregation in vitro. J Neurochem 1993; 61: 298–305
   PubMed Web of Science ®Google Scholar
• McLaurin J, Franklin T, Chakrabartty A, Fraser P E. Phosphatidyl and inositol involvement in Alzheimer amyloid-β fibril growth and arrest. J Mol Biol 1998; 278: 183–194
   PubMed Web of Science ®Google Scholar
• McLaurin J, Franklin T, Fraser P E, Chakrabartty A. Structural transitions associated with the interaction of Alzheimer β-amyloid peptides with gangliosides. J Biol Chem 1998; 273: 4506–4515
   PubMed Web of Science ®Google Scholar