A spectroscopic study of some of the peptidyl radicals formed following hydroxyl radical attack on β-amyloid and α-synuclein

References

• Walsh DM, Hartley DM, Kusumoto Y, Fezoui Y, Condron MM, Lomakin A, Benedek GB, Selkoe DJ, Teplow DB. Amyloid β-protein fibrillogenesis. Structure and biological activity. J Biol Chem 1999; 274: 25945–25952
   PubMed Web of Science ®Google Scholar
• Kayed R, Head E, Thompson JL, McIntire TM, Milton SC, Cotman CW, Glabe CG. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 2003; 300: 486–489
   PubMed Web of Science ®Google Scholar
• Stefani M, Dobson CM. Protein aggregation and aggregate toxicity: New insights into protein folding misfolding diseases and biological evolution. J Mol Med 2003; 81: 678–699
   PubMed Web of Science ®Google Scholar
• Chromy BA, Nowak RJ, Lambert MP, Viola KL, Chang L, Velasco PT, Jones BW, Fernandez SJ, Lacor PN, Horowitz P, Finch CE, Krafft GA, Klein WL. Self-assembly of Aβ(1–42) into globular neurotoxins. Biochemistry 2003; 42: 12749–12760
   PubMed Web of Science ®Google Scholar
• Glaser CB, Yamin G, Uversky VN, Fink AL. Methionine oxidation, α-synuclein and Parkinson's disease. Biochim Biophys Acta 2005; 1703: 157–169
   PubMedGoogle Scholar
• Nunomura A, Perry G, Aliev G, Hirai K, Takeda A, Balraj EK, Jones PK, Ghanbari H, Wataya T, Shimohama S, Chiba S, Atwood CS, Petersen RB, Smith MA. Oxidative damage is the earliest event in Alzheimer disease. J Neuropathol Exp Neurol 2001; 60: 759–767
   PubMed Web of Science ®Google Scholar
• Beal MF. Oxidative damage as an early marker of Alzheimer's disease and mild cognitive impairment. Neurobiol Aging 2005; 26: 585–586
   PubMedGoogle Scholar
• Keller JN, Schmitt FA, Scheff SW, Ding Q, Chen Q, Butterfield DA, Markesbury WR. Evidence of increased oxidative damage in subjects with mild cognitive impairment. Neurology 2005; 64: 1152–1156
   PubMed Web of Science ®Google Scholar
• Markesbery WR. Oxidative stress hypothesis in Alzheimer's disease. Free Radic Biol Med 1997; 23: 134–147
   PubMed Web of Science ®Google Scholar
• Miranda S, Opazo C, Larrondo LF, Muñoz FJ, Ruiz F, Leighton F, Inestrosa NC. The role of oxidative stress in the toxicity induced by amyloid β-peptide in Alzheimer's disease. Prog Neurobiol 2000; 62: 633–648
   PubMed Web of Science ®Google Scholar
• Sayre LM, Smith MA, Perry G. Chemistry and biochemistry of oxidative stress in neurodegenerative disease. Curr Med Chem 2001; 8: 721–738
   PubMed Web of Science ®Google Scholar
• Butterfield DA, Drake J, Pocernich C, Castegna A. Evidence of oxidative damage in Alzheimer's disease brain: Central role for amyloid β-peptide. Trends Mol Med 2001; 7: 548–554
   PubMed Web of Science ®Google Scholar
• Beal MF. Oxidatively modified proteins in aging and disease. Free Radic Biol Med 2002; 32: 797–803
   PubMed Web of Science ®Google Scholar
• Barnham KJ, Masters CL, Bush AI. Neurodegenerative diseases and oxidative stress. Nat Rev Drug Discov 2004; 3: 205–214
   PubMed Web of Science ®Google Scholar
• Huang XD, Atwood CS, Hartshorn MA, Multhaup G, Goldstein LE, Scarpa RC, Cuajungco MP, Gray DN, Lim J, Moir RD, Tanzi RE, Bush AI. The Aβ peptide of Alzheimer's disease directly produces hydrogen peroxide through metal ion reduction. Biochemistry 1999; 38: 7609–7616
   PubMed Web of Science ®Google Scholar
• Huang XD, Cuajungco MP, Atwood CS, Hartshorn MA, Tyndall JDA, Hanson GR, Stokes KC, Leopold M, Multhaup G, Goldstein LE, Scarpa RC, Saunders AJ, Lim J, Moir RD, Glabe C, Bowden EF, Masters CL, Fairlie DP, Tanzi RE, Bush AI. Cu(II) potentiation of Alzheimer Aβ neurotoxicity—correlation with cell-free hydrogen peroxide production and metal reduction. J Biol Chem 1999; 274: 37111–37116
   PubMed Web of Science ®Google Scholar
• Atwood CS, Scarpa RC, Huang XD, Moir RD, Jones WD, Fairlie DP, Tanzi RE, Bush AI. Characterization of copper interactions with Alzheimer amyloid β peptides: Identification of an attomolar-affinity copper binding site on amyloid β 1–42. J Neurochem 2000; 75: 1219–1233
   PubMed Web of Science ®Google Scholar
• Miura T, Suzuki K, Takeuchi H. Binding of iron(III) to the single tyrosine residue of amyloid β-peptide probed by Raman spectroscopy. J Mol Struct 2001; 598: 79–84
   Google Scholar
• Curtain CC, Ali F, Volitakis I, Cherny RA, Norton RS, Beyreuther K, Barrow CJ, Masters CL, Bush AI, Barnham KJ. Alzheimer's disease amyloid-β binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits. J Biol Chem 2001; 276: 20466–20473
   PubMed Web of Science ®Google Scholar
• Opazo C, Barría MI, Ruiz FH, Inestrosa NC. Copper reduction by copper binding proteins and its relation to neurodegenerative diseases. BioMetals 2003; 16: 91–98
   PubMedGoogle Scholar
• Behl C, Davis JB, Lesley R, Schubert D. Hydrogen peroxide mediates amyloid-β protein toxicity. Cell 1994; 77: 817–827
   PubMed Web of Science ®Google Scholar
• Turnbull S, Tabner BJ, El-Agnaf OMA, Allsop D. α-Synuclein implicated in Parkinson's disease catalyses the formation of hydrogen peroxide in vitro. Free Radic Biol Med 2001; 30: 1163–1170
   PubMed Web of Science ®Google Scholar
• Tabner BJ, Turnbull S, El-Agnaf OMA, Moore S, Davies Y, Allsop D. Production of reactive oxygen species from aggregating proteins implicated in Alzheimer's disease, Parkinson's disease and other neurodegenerative diseases. Curr Top Med Chem 2001; 1: 507–517
   PubMedGoogle Scholar
• Tabner BJ, Turnbull S, El-Agnaf OMA, Allsop D. Formation of hydrogen peroxide and hydroxyl radicals from Aβ and α-synuclein as a possible mechanism of cell death in Alzheimer's disease and Parkinson's disease. Free Radic Biol Med 2002; 32: 1076–1083
   PubMed Web of Science ®Google Scholar
• Tabner BJ, Turnbull S, El-Agnaf OMA, Allsop D. Direct production of reactive oxygen species from aggregating proteins and peptides implicated in the pathogenesis of neurodegenerative diseases. Curr Med Chem—Immunol Endocr Metab Agents 2003; 3: 299–308
   Google Scholar
• Tabner BJ, El-Agnaf OMA, Turnbull S, German MJ, Paleologou KE, Hayashi Y, Cooper LJ, Fullwood NJ, Allsop D. Hydrogen peroxide is generated during the very early stages of aggregation of the amyloid peptides implicated in Alzheimer disease and familial British dementia. J Biol Chem 2005; 280: 35789–35792
   PubMed Web of Science ®Google Scholar
• Turnbull S, Tabner BJ, Brown DR, Allsop D. Copper-dependent generation of hydrogen peroxide from the toxic prion protein fragment PrP106–126. Neurosci Lett 2003; 336: 159–162
   PubMed Web of Science ®Google Scholar
• Turnbull S, Tabner BJ, Brown DR, Allsop D. Generation of hydrogen peroxide from mutant forms of the prion protein fragment PrP121-231. Biochemistry 2003; 42: 7675–7681
   PubMedGoogle Scholar
• Turnbull S, Tabner BJ, Brown DR, Allsop D. Quinacrine acts as an antioxidant and reduces the toxicity of the prion peptide PrP106-126. Neuroreport 2003; 14: 1743–1745
   PubMed Web of Science ®Google Scholar
• Schöneich C. Methionine oxidation by reactive oxygen species: Reaction mechanisms and relevance to Alzheimer's disease. Biochim Biophys Acta 2005; 1703: 111–119
   PubMed Web of Science ®Google Scholar
• Naslund J, Schierhorn A, Hellman U, Lannfelt L, Roses AD, Tjernberg LO, Silberring J, Gandy SE, Winblad B, Greengard P, Norstedt C, Terenius L. Relative abundance of Alzheimer Aβ amyloid peptide variants in Alzheimer's disease and normal aging. Proc Natl Acad USA 1994; 91: 8378–8382
   PubMed Web of Science ®Google Scholar
• Dong J, Atwood CS, Anderson VE, Siedlak SL, Smith MA, Perry G, Carey PR. Metal binding and oxidation of amyloid-β within isolated senile plaque cores: Raman microscopic evidence. Biochemistry 2003; 42: 2768–2773
   PubMed Web of Science ®Google Scholar
• Davies MJ, Hawkins CL. EPR spin trapping of protein radicals. Free Radic Biol Med 2004; 36: 1072–1086
   PubMed Web of Science ®Google Scholar
• Nakao LS, Iwai LK, Kalil J, Augusto O. Radical production from free and peptide-bound methionine sulfoxide oxidation by peroxynitrite and hydrogen peroxide/iron(II). FEBS Lett 2003; 547: 87–91
   PubMed Web of Science ®Google Scholar
• Hensley K, Carney JM, Mattson MP, Aksenova M, Harris M, Wu JF, Floyd RA, Butterfield DA. A model for β-amyloid aggregation and neurotoxicity based on free-radical generation by the peptide: Relevance to Alzheimer disease. Proc Natl Acad Sci USA 1994; 91: 3270–3274
   PubMed Web of Science ®Google Scholar
• El-Agnaf OMA, Goodwin H, Sheridan JM, Frears ER, Austen BM. Improved solid phase syntheses of amyloid proteins associated with neurodegenerative diseases. Protein Pept Lett 2000; 7: 1–8
   Google Scholar
• Kaur H, Leung KHW, Perkins MJ. A water-soluble nitroso-aromatic spin-trap. J Chem Soc Chem Commun 1981; 142–143
   Google Scholar
• Duling DR. Simulation of multiple isotropic spin-trap EPR-spectra. J Magn Reson B 1994; 104: 105–110
   PubMedGoogle Scholar
• Davies MJ. The oxidative environment and protein damage. Biochim Biophys Acta 2005; 1703: 93–109
   PubMed Web of Science ®Google Scholar
• Lagercrantz C, Forshult S. Trapping of short-lived free radicals as nitroxide radicals detectable by ESR spectroscopy. Radicals formed in reaction between OH-radicals and some sulphoxides and sulphones. Acta Chem Scand 1969; 23: 811–817
   Google Scholar
• Schöneich C, Pogocki D, Hug GL, Bobrowski B. Free radical reactions of methionine in peptides: Mechanisms relevant to β-amyloid oxidation and Alzheimer's disease. J Am Chem Soc 2003; 125: 13700–13713
   PubMed Web of Science ®Google Scholar
• Butterfield DA, Bush AI. Alzheimer's amyloid β-peptide (1–42): Involvement of methionine residue 35 in the oxidative stress and neurotoxicity properties of this peptide. Neurobiol Aging 2004; 25: 563–568
   PubMed Web of Science ®Google Scholar
• Ali FE, Leung A, Cherny RA, Mavros C, Barnham KJ, Separovic F, Barrow CJ. Dimerisation of N-acetyl-1-tyrosine ethyl ester and Aβ peptides via formation of dityrosine. Free Radic Res 2006; 40: 1–9
   PubMed Web of Science ®Google Scholar