Alzheimer's β-amyloid peptide as a source of neurotoxic free radicals: The role of structural effects

Acta Neurobiologiae Experimentalis

Volumn 63, Issue 2, 2003, Pages 131-145

  Pogocki, Dariusz ^a  

^a INSTITUTE OF NUCLEAR CHEMISTRY AND TECHNOLOGY   (Poland)

Author keywords

amyloid; Ageing; Alzheimer's disease; Copper; Free radicals; Histidine; Hydroxyl radical; Methionine; Methionine sulphoxide; One electron oxidation; Oxidative stress; Peptides; Reactive oxygen species; Sulphide radical cation; Thiyl radicals

Indexed keywords

AMYLOID BETA PROTEIN; COPPER ION; FREE RADICAL; METHIONINE; REACTIVE OXYGEN METABOLITE;

AGING; ALZHEIMER DISEASE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CONFERENCE PAPER; CYTOTOXICITY; DISEASE ASSOCIATION; NEUROTOXICITY; OXIDATION; OXIDATION REDUCTION REACTION; OXIDATIVE STRESS; PATHOGENESIS; PROTEIN SECONDARY STRUCTURE;

ALZHEIMER DISEASE; AMYLOID BETA-PROTEIN; FREE RADICALS; HUMANS; NEURONS; OXIDATIVE STRESS; PROTEIN STRUCTURE, SECONDARY; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0037980148     PISSN: 00651400     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Conference Paper

References (198)

1. Akhlaq M.S., Schuchmann H.-P., von Sonntag C. (1987) The reverse of the 'repair' reaction of thiols: H-abstraction at carbon by thiyl radicals. Int J Radiat Biol 51: 91-102.
2. Aksenov M., Aksenova M., Butterfield A.D., Hensley K., Vigo-Pelfrey C., Carney J.M. (1996) Glutamine synthetase-induced neurotoxicity accompained by abrogation of fibril formation and amyloid β-peptide fragmentation. J Neurochem 66: 2050-2056.
3. 2+ binding sites in the N-terminal domain of the prion protein by EPR and CD spectroscopy. Biochemistry 39: 13760-13771.
4. Asmus K.-D. (1979) Stabilization of oxidized sulfur centers inorganic sulfides. Radical cations and odd-electron sulfur-sulfur bonds. Acc Chem Res 12: 436-442.
5. Asmus K.-D. (1990) Sulfur-centered three electron bonded radical species. In: Sulfur-centered reactive intermediates in chemistry and biology (Eds. C. Chatgilialoglu and K.-D. Asmus). Plenum Press, New York, p. 155-172.
6. Atwood C.S., Huang X., Khatri A., Scarpa R.C., Kim Y.S., Moir R.D., Tanzi R.E., Roher A.E., Bush A.I. (2000) Copper catalyzed oxidation of Alzheimer Aβ. Cell Mol Biol (Noisy -le-grand) 46: 777-783.
7. Atwood C.S., Huang X., Moir R.D., Tanzi R.E., Bush A.I. (1999) Role of free radicals and metal ions in the pathogenesis of Alzheimer's disease. Met Ions Biol Syst 36: 309-364.
8. Baciocchi E., Rol C., Mandolini L. (1980) Changeover from rate-determining electron transfer to rate-determining proton transfer in the oxidation of alkyl aromatic compounds by ceric ammonium nitrate. J Am Chem Soc 102: 7597-7598.
9. Balbach J.J., Ishii Y., Antzutkin O.N., Leapman R.D., Rizzo N.W., Dyda F., Reed J., Tycko R. (2000) Amyloid fibril formation by Aβ16-22, a seven-residue fragment of the Alzheimer's β-amyloid peptide, and structural characterization by solid state NMR. Biochemistry 39: 13748-13759.
10. Barcikowska M. (1999) Clinical pattern of early phase of Alzheimer's disease. Neurol Neurochir Pol Suppl 1: 29-37.
11. Beyreuther K., Bush A.I., Dyrks T., Hilbich C., Konig G., Monning U., Multhaup G., Prior R., Rumble B., Schubert W. (1991) Mechanisms of amyloid deposition in Alzheimer's disease. Ann N Y Acad Sci 640: 129-139.
12. Blain H., Jeandel C. (1998) Alzheimer disease. Epidemiology, genetics and physiopathological hypotheses. Presse Med 27: 725-730.
13. Bobrowski K., Hug G.L., Marciniak B., Miller B.L., Schöneich C. (1997) Mechanism of one-electron oxidation of β-, γ-, and δ-hydroxyalkyl sulfides. Catalysis through intramolecular proton transfer and sulfur-oxygen bond formation. J Am Chem Soc 119: 8000-8011.
14. Bobrowski, K., Pogocki, D., Schöneich, C., Hug, G. L., Marciniak, B. (2003) Sulfur-radical cation-peptide bond complex in the one-electrqn oxidation of S-alkylglutationes. J Am Chem Soc (in preparation).
15. Bondi A.J. (1964) Van der Waals volumes and radii. J Phys Chem 68: 441-451.
16. Bonifacic M., Weiss J., Chaudhri S.A., Asmus K.-D. (1985) Oxidation of thiols by radical cations of organic sulfides. J Phys Chem 89: 3910-3914.
17. Brown C.M., Wright E., Colton C.A., Sullivan P.M., Laskowitz D.T., Vitek M.P. (2002) Apolipoprotein E isoform mediated regulation of nitric oxide release. Free Radic Biol Med 32: 1071-1075.
18. Brown D.R. (2002) Copper and prion diseases. Biochem Soc Trans 30: 742-745.
19. Brown D.R., Schmidt B., Kretzschmar H.A. (1998) Effects of copper on survival of prion protein knockout neurons and glia. J Neurochem 70: 1686-1693.
20. Brown D.R., Wong B.S., Hafiz F., Clive C., Haswell S.J., Jones I.M. (1999) Normal prion protein has an activity like that of superoxide dismutase. Biochem J 344: 1-5.
21. Buchet R., Pikuła S. (2000) Alzheimer's disease: its origin at the membrane, evidence and questions. Acta Biochim Pol 47: 725-733.
22. Burling F.T., Goldstein B.M. (1992) Computational studies of nonbonded sulfur-oxygen and selenium-oxygen interactions in the thiazole and selenazole nucleosides. J Am Chem Soc 114: 2313-2320.
23. Burns C.S., Aronoff-Spencer E., Dunham C.M., Lario P., Avdievich N.I., Antholine W.E., Olmstead M.M., Vrielink A., Gerfen G.J., Peisach J., Scott W.G., Millhauser G.L. (2002) Molecular features of the copper binding sites in the octarepeat domain of the prion protein. Biochemistry 41: 3991-4001.
24. Bush A.I. (2000) Metals and neuroscience. Curr Opin Chem Biol 4: 184-191.
25. Butterfield A.D. (1996) Commentary: Alzheimer's disease: a disorder of oxidative stress. Alzheimer's Dis Rev 1: 68-70.
26. Butterfield A.D. (1997) β-Amyloid-associated free radical oxidative stress and neurotoxicity: implications for Alzheimer's disease. Chem Res Toxicol 10: 495-506.
27. Butterfield A.D., Drake J., Pocernich C., Castagena A. (2001) Evidence of oxidative damage in Alzheimer's disease brain: central role for amyloid β-peptide. Trends Mol Med 7: 548-554.
28. Butterfield D.A., Hensley K., Harris M., Mattson M., Carney J. (1994) β-Amyloid peptide free radical fragments initiate synaptosomal lipoperoxidation in a sequence-specific fashion: implications to Alzheimer's disease. Biochem Biophys Res Commun 200: 710-715.
29. Butterfield D.A., Lauderback C.M. (2002) Lipid peroxidation and protein oxidation in Alzheimer's disease brain: potential causes and consequences involving amyloid β-peptide- associated free radical oxidative stress. Free Radic Biol Med 32: 1050-1060.
30. 2+, nitroxide spin probes, and synaptosomal membrane proteins. Life Sci 58: 217-228.
31. Cadenas E., Packer L. (1999) Understanding the process of aging. The roles of mitochondria, free radicals, antioxidants (Eds. E. Cadenas and L. Packer). Marcel Dekker Inc., New York, 366 p.
32. Carter N.K., Taverner T., Schiesser C.H., Greenberg M.M. (2000) Chemical evidence for thiyl radical addition to the C6-position of pyrimidine nucleoside and its possible relevance to DNA damage amplification. J Org Chem 65: 8375-8378.
33. Chatgilialoglu C., Ferreri C., Ballestri M., Mulazzani Q.G., Landi L. (2000) Cis-trans isomerization of monounsaturated fatty acid residues in phospholipids by thiyl radicals. J Am Chem Soc 122: 4593-4601.
34. Cherny R.A., Atwood C.S., Xilinas M.E., Gray D.N., Jones W.D., McLean C.A., Barnham K.J., Volitakis I., Fraser F.W., Kim Y., Huang, X., Goldstein L.E., Moir R.D., Lim J.T., Beyreuther K., Zheng H., Tanzi R.E., Masters C.L., Bush A.I. (2001) Treatment with a copper-zinc chelator markedly and rapidly inhibits β-amyloid accumulation in Alzheimer's disease transgenic mice. Neuron 30: 665-676.
35. Cherny R.A., Barnham K.J., Lynch T., Volitakis I., Li Q.X., McLean C.A., Multhaup G., Beyreuther K., Tanzi R.E., Masters C.L., Bush A.I. (2000) Chelation and intercalation: complementary properties in a compound for the treatment of Alzheimer's disease. J Struct Biol 130: 209-216.
36. Christen Y. (2000) Oxidative stress and Alzheimer disease. Am J Clin Nutr 71: 621S-629S.
37. Clark T. (1988) Odd-electron σ bonds. J Am Chem Soc 110: 1672-1678.
38. Clarke R., Smith A.D., Jobst K.A., Refsum H., Sutton L., Ueland P.M. (1998) Folate, vitamin B12, and serum total homocysteine levels in confirmed Alzheimer disease. Arch Neurol 55: 1449-1455.
39. Coles M., Bicknell W., Watson A.A., Fairlie D.P., Craik D.J. (1998) Solution structure of amyloid β-peptide(1-40) in a water-micelle environment. Is the membrane-spanning domain where we think it is? Biochemistry 37: 11064-11077.
40. Cuajungco M.P., Faget K.Y., Huang X., Tanzi R.E., Bush A.I. (2000) Metal chelation as a potential therapy for Alzheimer's disease. Ann N Y Acad Sci 920: 292-304.
41. Curtain C.C., Ali F., Volitakis I., Chemy R.A., Norton R.S., Beyreuther K., Barrow C.J., Masters C.L., Bush A.I., Barnham K.J. (2001) 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 276: 20466-20473.
42. Cutler R.G., Packer L., Bertram J., Mori A. (1995) Oxidative stress and aging (Eds. R.G. Cutler, L. Packer, J. Bertram and A. Mori). Birkhäuser Verlag, Basel, 396 p.
43. Davies K.J.A. (1992) Oxidative damage and repair. Chemical, biological and medicinal aspects (Eds. K.J.A. Davies). Pergamon Press, New York, 889 p.
44. Diaz-Arrastia R. (1998) Hyperhomocysteinemia: a new risk factor for Alzheimer disease? Arch Neurol 55: 1407-1408.
45. Durell S.R., Guy H.R., Arispe N., Rojas E., Pollard H.B. (1994) Theoretical models of the ion channel structure of amyloid β-protein. Biophys J 67: 2137-2145.
46. Dworakowska B., Dołowy K. (2000) Ion channels-related diseases. Acta Biochim Pol 47: 685-703.
47. Evans P., Harrington C. (1998) Aluminosilicate particulate and β-amyloid in vitro interactions: a model of Alzheimer plaque formation. Biochem Soc Trans 26: S251.
48. Evans P.H., Klinowski J., Yano E., Urano N. (1989) Alzheimer's disease: a pathogenic role for aluminosilicate-induced phagocytic free radicals. Free Radic Res Commun 6: 317-321.
49. Evans P.H., Yano E., Klinowski J., Peterhans E. (1992) Oxidative damage in Alzheimer's dementia, and the potential etiopathogenic role of aluminosilicates, microglia and micronutrient interactions. EXS 62: 178-189.
50. Ferencik M., Novak M., Rovensky J., Rybar I. (2001) Alzheimer's disease, inflammation and non-steroidal anti-inflammatory drugs. Bratisl Lek Listy 102: 123-132.
51. Ferreri C., Costantino C., Landi L., Mulazzani Q.G., Chatgilialoglu C. (1999) The thiyl radical-mediated isomerization of cis-monounsaturated fatty acid residues in phospholipids: a novelpath of membrane damage? J Chem Soc Chem Commun p.407-408.
52. Flitter W., Rowley D.A., Halliwell B. (1983) Superoxide-dependent formation of hydroxyl radicals in the presence of iron salts. What is the physiological iron chelator? FEBS Lett 158: 310-312.
53. Fox S., Karlin K.D. (1995) Dioxygen reactivity in copper proteins and complexes. In: Active oxygen in biochemistry (Eds. J. Selverstone Valentine, C.S. Foote, A. Greenberg and J.F. Liebman). Blackie Academic & Professional, Glasgow, p. 188-231.
54. Gabryelewicz T. (1999) Prevalence of dementia syndromes. Neurol Neurochir Pol Suppl 1: 11-17.
55. Garcia J.I., Mayoral J.A., Salvatella L. (2000) Do secondary orbitals interactions really exist? Acc Chem Res 33: 658-664.
56. Gibson G.E. (2002) Interactions of oxidative stress with cellular calcium dynamics and glucose metabolism in Alzheimer's disease. Free Radic Biol Med 32: 1061-1070.
57. Glass R.S., Duchek J.R., Klug J., Wilson D. (1977) Facilitation of dialkyl sulfide oxidation by neighboring groups. J Am Chem Soc 99: 7349-7350.
58. Glass R.S., Petsom A., Hojjatie M., Coleman B.R., Duchek J.R., Klug J., Wilson G.S. (1988) Facilitation of electrochemical oxidation of dialkyl sulfides appended with neighboring carboxylate and alcohol group. J Am Chem Soc 110: 4772-4778.
59. Grant W.B. (1997) Dietary links to Alzheimer's disease. Alzheimer's Dis Rev 2: 42-55.
60. Haass C., Koo E.H., Mellon A., Hung A.Y., Selkoe D.J. (1992) Targeting of cell-surface β-amyloid precursor protein to lysosomes: alternative processing into amyloid-bearing fragments. Nature 357: 500-503.
61. Halliwell B., Gutteridge J.M. (1999) Free radicals in biology and medicine. Oxford University Press, Oxford, 936 p.
62. Hardy J., Selkoe D.J. (2002) The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297: 353-356.
63. Harris M.E., Hensley K., Butterfield D.A., Leedle R.A., Carney J.M. (1995) Direct evidence of oxidative injury produced by the Alzheimer's β-amyloid peptide (1-40) in cultured hippocampal neurons. Exp Neurol 131: 193-202.
64. Heinecke J.W. (2002) Oxidized amino acids: culprits in human atherosclerosis and indicators of oxidative stress. Free Radic Biol Med 32: 1090-1101.
65. Henderson V.W., Finch C.E. (1989) The neurobiology of Alzheimer's disease. J Neurosurg 70: 335-353.
66. Hensley K., Aksenova M., Carney J.M., Harris M., Butterfield D.A. (1995b) Amyloid β-peptide spin trapping. II: Evidence for decomposition of the PBN spin adduct. Neuroreport 6: 493-496.
67. Hensley K., Butterfield D.A., Mattson M., Aksenova M., Harris M., Wu J.F., Floyd R., Carney J. (1995a) A model for β-amyloid aggregation and neurotoxicity based on the free radical generating capacity of the peptide: implications of "molecular shrapnel" for Alzheimer's disease. Proc West Pharmacol Soc 38: 113-120.
68. Hensley K., Carney J.M., Mattson M.P., Aksenova M., Harris M., Wu J.F., Floyd R.A., Butterfield D.A. (1994) A model for β-amyloid aggregation and neurotoxicity based on free radical generation by the peptide: relevance to Alzheimer disease. Proc Natl Acad Sci U S A 91: 3270-3274.
69. Hiller K.-O., Masloch B., Göbl M., Asmus K.-D. (1981) Mechanism of the OH radical induced oxidation of methionine in aqueous solution. J Am Chem Soc 103: 2734-2743.
70. Huang X., Atwood C.S., Hartshorn M.A., Multhaup G., Goldstein L.E., Scarpa R.C., Cuajungco M.P., Gray D.N., Lim J., Moir R.D., Tanzi R.E., Bush A.I. (1999a) The Aβ peptide of Alzheimer's disease directly produces hydrogen peroxide through metal ion reduction. Biochemistry 38: 7609-7616.
71. Huang X., Atwood C.S., Moir R.D., Hartshorn M.A., Vonsattel J.P., Tanzi R.E., Bush A.I. (1997) Zinc-induced Alzheimer's Aβ 1-40 aggregation is mediated by conformational factors. J Biol Chem 272: 26464-26470.
72. Huang X., Cuajungco M.P., Atwood C.S., Hartshorn M.A., Tyndall J.D., Hanson G.R., Stokes K.C., Leopold M., Multhaup G., Goldstein L.E., Scarpa R.C., Saunders A.J., Lim J., Moir R.D., Glabe C., Bowden E.F., Masters C.L., Fairlie D.P., Tanzi R.E., Bush A.I. (1999b) Cu(II) potentiation of alzheimer Aβ neurotoxicity. Correlation with cell-free hydrogen peroxide production and metal reduction. J Biol Chem 274: 37111-37116.
73. Huang X., Cuajungco M.P., Atwood C.S., Moir R.D., Tanzi R.E., Bush A.I. (2000) Alzheimer's disease, β-amyloid protein and zinc. J Nutr 130: 1488S-1492S.
74. Kański J., Aksenova M., Schöneich C., Butterfield D.A. (2002) Substitution of isoleucine-31 by helical-breaking proline abolishes oxidative stress and neurotoxic properties of Alzheimer's amyloid β-peptide (1-42). Free Radic Biol Med 32: 1205-1211.
75. Kontush A. (2001a) Amyloid-β: an antioxidant that becomes a pro-oxidant and critically contributes to Alzheimer's disease. Free Radic Biol Med 31: 1120-1131.
76. Kontush A. (2001b) Alzheimer's amyloid-β as a preventive antioxidant for brain lipoproteins. Cell Mol Neurobiol 21: 299-315.
77. Kontush A., Berndt C., Weber W., Akopyan V., Arlt S., Schippling S., Beisiegel U. (2001b) Amyloid-β is an antioxidant for lipoproteins in cerebrospinal fluid and plasma. Free Radic Biol Med 30: 119-128.
78. Kontush A., Donarski N., Beisiegel U. (2001a) Resistance of human cerebrospinal fluid to in vitro oxidation is directly related to its amyloid-β content. Free Radic Res 35: 507-517.
79. Koppaka V., Axelsen P.H. (2000) Accelerated accumulation of amyloid β proteins on oxidatively damaged lipid membranes. Biochemistry 39: 10011-10016.
80. 2-treated Cu Zn-SOD protein with LC-ES-Q-TOF-MS, MS/MS for the determination of the copper-binding site. J Am Chem Soc 123: 9268-9278.
81. 1H NMR of Aβ -amyloid peptide congeners in water solution. Conformational changes correlate with plaque competance. Biochemistry 34: 5191-5200.
82. Lorenzo A., Yankner B.A. (1994) β-Amyloid neurotoxicity requires fibrils formation and is inhibited by Congo red. Proc Natl Acad Sci U S A 91: 12243-12247.
83. Lovell M.A., Robertson J.D., Teesdale W.J., Campbell J.L., Markesbery W.R. (1998) Copper, iron and zinc in Alzheimer's disease senile plaques. J Neurol Sci 158: 47-52.
84. Lynch T., Cherny R.A., Bush A.I. (2000) Oxidative processes in Alzheimer's disease: the role of Aβ-metal interactions. Exp Gerontol 35: 445-451.
85. 2+ homeostasis and cell death. J Neurosci 15: 6239-6249.
86. Markesbery W.R. (1997) Oxidative stress hypothesis in Alzheimer's disease. Free Radic Biol Med 23: 134-147.
87. Mattson M.P. (1997a) Central role of oxyradicals in the mechanism of amyloid β-peptide cytotoxicity. Alzheimer's Dis Rev 2: 1-14.
88. Mattson M.P. (1997b) Cellular action of β-amyloid precursor protein and its soluble and fibrillogenic derivatives. Physiol Rev 77: 1081-1082.
89. Mattson M.P., Mark R.J., Furukawa K., Bruce A.J. (1997) Disruption of brain cell ion homeostasis in Alzheimer's disease by oxy radicals, and signalling pathways that protect therefrom. Chem Res Toxicol 10: 507-517.
90. McDowell I. (2001) Alzheimer's disease: insights from epidemiology. Aging (Milano) 13: 143-162.
91. McLaurin J., Chakrabartty A. (1996) Membrane disruption by Alzheimer β-amyloid peptides mediated through specific binding to either phospholipids or gangliosides. Implications for neurotoxicity. J Biol Chem 271: 26482-26489.
92. Miller B., Kuczera K., Schöneich C. (1998) One-electron photooxidation of N-methionyl peptides. Mechanism of sulfoxide and azasulfonium diastereomer formation through reaction of sulfide radical cation complex with oxygen and superoxide. J Am Chem Soc 120: 3345-3356.
93. Miller B., Williams T.D., Schöneich C. (1996) Mechanism of sulfoxide formation through reaction of sulfur radical cation complexes with superoxide or hydroxide ion in oxygenated aqueous solution. J Am Chem Soc 118: 11014-11025.
94. Miranda S., Opazo C., Larrondo L.F., Munoz F.J., Ruiz F., Leighton F., Inestrosa N.C. (2000) The role of oxidative stress in the toxicity induced by amyloid β-peptide in Alzheimer's disease. Prog Neurobiol 62: 633-648.
95. Miura T., Suzuki K., Kohata N., Takeuchi H. (2000) Metal binding modes of Alzheimer's amyloid β-peptide in insoluble aggregates and soluble complexes. Biochemistry 39: 7024-7031.
96. Mosharov E., Cranford M.R., Banerjee R. (2000) The quantitatively important relationship between homocysteine metabolism and glutathione synthesis by the transsulfuration pathway and its regulation by redox changes. Biochemistry 39: 13005-13011.
97. Nagao Y., Hirata T., Goto S., Sano S., Kakehi A., Iizuka K., Shiro M. (1998) Intramolecular nonbonded SO interaction recognized in (acylimino)thiadiazoline derivatives as angiotensin II receptor antagonists and related compounds. J Am Chem Soc 120: 3104-3110.
98. Nauser T., Schöneich C. (2003) Thiyl radicals abstract hydrogen atoms from αC-H bonds in model peptides: Absolute rate constants and effect of amino acid structure. J Am Chem Soc 125: 2042-2043.
99. Näslund J., Haroutunian V., Mosh R., Davis K.L., Davis P., Greengard P., Buxbaum J.D. (2000) Correlation between elevated levels of amyloid β-peptide in the brain and cognitive decline. JAMA 283: 1571-1577.
100. Näslund J., Schierhorn A., Hellman U., Lannfelt L., Roses A.D., Tjernberg L.O., Silberring J., Gandy S.E., Winblad B., Greengard P., Nordstedt C., Terenius L. (1994) Relative abundance of Alzheimer Aβ amyloid peptide variants in Alzheimer disease and normal aging. Proc Natl Acad Sci U S A 91: 8378-8382.
101. Oda T., Wals P., Osterbung H., Johnson S., Pasinetti G., Morgan T., Rozovosky I., Stein W.B., Synder S., Holzman T., Kraft G., Finch C. (1995) Clusterin (apo J) alters the aggregation of amyloid β peptide (1-42) and forms slowly sedimenting Aβ complexes that cause oxidative stress. Eur Neurol 136: 22-31.
102. Pal You B. (1993) Free radicals in aging (Ed. B. Pal You). CRC Press, Boca Raton, 303 p.
103. Pike C.J., Walencewicz-Wasserman A.J., Glabe C.G., Cotman C.W. (1991) Aggregation related toxicity of synthetic β-amyloid protein in hippocampal cultures. Eur J Pharmacol 207: 367-368.
104. n-Met peptides. J Phys Chem B 105: 1250-1259.
105. Pogocki D., Schöneich C. (2000) Chemical stability of nucleic acid-derived drugs. J Pharm Sci 89: 443-456.
106. Pogocki D., Schöneich C. (2001) Thiyl radicals abstract hydrogen atoms from carbohydrates: reactivity and selectivity. Free Radic Biol Med 31: 98-107.
107. Pogocki D., Schöneich C. (2002a) Computational characterization of sulfur-oxygen-bonded sulfuranyl radicals derived from a alkyl- and (carboxyalkyl)thopropionic acids: evidence for σ*-type radicals. J Org Chem 67: 1526-1535.
108. 35 in neurotoxic β-amyloid peptide. A molecular modeling study. Chem Res Toxicol 15: 408-418.
109. Pogocki D., Serdiuk K., Schöneich C. (2003) Computational characterization of sulfur-oxygen three-electron-bonded radicals in methionine and methionine-containing peptides: Important intermediates in one-electron oxidation processes. J Phys Chem A (in press).
110. Pryor W.A., Gojon G., Stanley J.P. (1973) Hydrogen abstraction by thiyl radicals. J Am Chem Soc 95: 945-946.
111. Rauk A., Armstrong D.A., Fairlie D.P. (2000a) Is oxidative damage by β-amyloid and prion peptides mediated by hydrogen atom transfer from glycine α-carbon to methionine sulfur within β-sheets? J Am Chem Soc 122: 9761-9767.
112. Rauk A., Yu D., Armstrong D.A. (1998) Oxidative damage to and by cysteine in proteins: an ab initio study of the radical structures, C-H, S-H, and C-C bond dissociation energies, and transition structures for H abstraction by thiyl radicals. J Am Chem Soc 120: 8848-8855.
113. Rauk A., Yu D., Armstrong D.A. (2000b) Influence of β-sheet structure on the susceptibility of proteins to backbone oxidative damage: Preference for αC-centered radical formation at glycine residues of antiparallel β-sheets. J Am Chem Soc 122: 4185-4192.
114. Reiersen H., Rees A.R. (2001) The hunchback and its neighbours: proline as an environmental modulator. Trends Biochem Sci 26: 679-684.
115. Riley P.A. (1994) Free radicals in biology: oxidative stress and the effects of ionizing radiation. Int J Radiat Biol 65: 27-33.
116. Robins M.J., Ewing G.J. (1999) Biomimetic modeling of the first substrate reaction at the active site of ribonucleotide reductases. Abstraction of H3' by a thiyl free radicals. J Am Chem Soc 121: 5823-5824.
117. Robinson S.R., Bishop G.L. (2002) A as a bioflocculant: implications for the amyloid hypothesis of Alzheimer's disease. Neurobiol Aging 5657: 1-22.
118. Rottkamp C.A., Nunomura A., Raina A.K., Sayre L.M., Perry G., Smith M.A. (2000) Oxidative stress, antioxidants, and Alzheimer disease. Alzheimer Dis Assoc Disord (Suppl.) 1: 62-66.
119. Rottkamp C.A., Raina A.K., Zhu X., Gaier E., Bush A.I., Atwood C.S., Chevion M., Perry G., Smith M.A. (2001) Redox-active iron mediates amyloid-β toxicity. Free Radic Biol Med 30: 447-450.
120. Rowan M.J. (1993) Recent research on the causes of Alzheimer's disease. Proc Nutr Soc 52: 255-262.
121. 2O. J Inorg Biochem 55: 87-99.
122. Savory J., Exley C., Forbes W.F., Huang Y., Joshi J.G., Kruck T., McLachlan D.R., Wakayama I. (1996) Can the controversy of the role of aluminum in Alzheimer's disease be resolved? What are the suggested approaches to this controversy and methodological issues to be considered? J Toxicol Environ Health 48: 615-635.
123. Sayre L.M., Perry G., Harris P.L.R., Liu Y., Schubert K.A., Smith M.A. (2000) In situ oxidative catalysis by neurofibrillary tangles an senile plaques in Alzheimer's disease: a central role for bound transition metals. J Neurochem 74: 270-279.
124. Sayre L.M., Zagorski M.G., Surewicz W.K., Krafft G.A., Perry G. (1997) Mechanisms of neurotoxicity associated with amyloid β deposition and the role of free radicals in the pathogenesis of Alzheimer's disease: a critical appraisal. Chem Res Toxicol 10: 518-526.
125. Schöneich C. (1995) Thiyl radicals, perthiyl radicals and oxidative reactions. In: Biothiols in health and disease (Eds. L. Packer and E. Cadenas). Marcel Dekker Inc., New York, p. 21-47.
126. Schöneich C. (2000) Mechanisms of metal-catalyzed oxidation of histidine to 2-oxo-histidine in peptides and proteins. J Pharm Biomed Anal 21: 1093-1097.
127. Schöneich C. (2001) Molecular aging. Exp Gerontol 36: 1423-1424.
128. Schöneich C. (2002) Redox processes of methionine relevant to β-amyloid oxidation and Alzheimer's disease. Arch Biochem Biophys 397: 370-376.
129. Schöneich C., Asmus K.-D., Bonifacic M. (1995) Determination of absolute rate constants for the reversible hydrogen-atom transfer between thiyl radicals and alcohols or ethers. J Chem Soc Faraday Trans 91: 1923-1930.
130. Schöneich C., Asmus K.D. (1990) Reaction of thiyl radicals with alcohols, ethers and polyunsaturated fatty acids: a possible role of thiyl free radicals in thiol mutagenesis? Radiat Environ Biophys. 29: 263-271.
131. Schöneich C., Bonifacic M., Asmus K.D. (1989) Reversible H-atom abstraction from alcohols by thiyl radicals: determination of absolute rate constants by pulse radiolysis. Free Radic Res Commun 6: 393-405.
132. Schöneich C., Bonifacic M., Dillinger U., Asmus K.-D. (1990) Hydrogen abstraction by thiyl radicals from activated C-H bonds of alcohols, ethers and polyunsaturated fatty acids. In: Sulfur-centered reactive intermediates in chemistry and biology (Eds. C. Chatgilialoglu and K.-D. Asmus). Plenum Press, New York, p. 367-387.
133. Schöneich C., Dillinger U., von Bruchhausen F., Asmus K.D. (1992) Oxidation of polyunsaturated fatty acids and lipids through thiyl and sulfonyl radicals: reaction kinetics, and influence of oxygen and structure of thiyl radicals. Arch Biochem Biophys 292: 456-467.
134. Schöneich C., Pogocki D., Hug G., Bobrowski K. (2003) Free radicals of methionine in peptides: mechanism relevant to β-amyloid oxidation in Alzheimer's disease. J Am Chem Soc (in press).
135. Schöneich C., Pogocki D., Wisniowski P., Hug G., Bobrowski K. (2000) Intramolecular sulfur-oxygen bond formation in radical cations of N-acetylmethionine amide. J Am Chem Soc 122: 10224-10225.
136. 6: Detection of 2-Oxo-histidine by HPLC-MS/MS. Chem Res Toxicol 15: 717-722.
137. aq. J Phys Chem 88: 3643-3647.
138. Schwinn J., Sprinz H., Drossler K., Leistner S., Brede O. (1998) Thiyl radical-induced cis/trans-isomerization of methyl linoleate in methanol and of linoleic acid residues in liposomes. Int J Radiat Biol 74: 359-365.
139. Seelig J., Lehrmann R., Terzi E. (1995) Domain formation induced by lipid-ion and lipid-peptide interactions. Mol Membr Biol 12: 51-57.
140. Selkoe D.J. (1996) Amyloid β-protein and the genetics of Alzheimer's disease. J Biol Chem 271: 18295-18298.
141. Seubert P., Vigo-Pelfrey C., Esch F., Lee M., Dovey H., Davis D., Sinha S., Schlossmacher M., Whaley J., Swindlehurst C. (1992) Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids. Nature 359: 325-327.
142. Shao H., Jao S., Ma K., Zagorski M.G. (1999) Solution structures of micelle-bound amyloid β-(1-40) and β-(1-42) peptides of Alzheimer's disease. J Mol Biol 285: 755-773.
143. Shimohigashi Y., Matsumoto H., Takano Y., Saito R., Iwata T., Kamiya H., Ohno M. (1993) Receptor-mediated specific biological activity of a β-amyloid protein fragment for NK-1 substance P receptors. Biochem Biophys Res Commun 193: 624-630.
144. Sies H. (1991) Oxidative stress: oxidants and antioxidants. Academic Press, New York, 650 p.
145. Simic M.G., Taylor K.A., Ward J.G., von Sonntag C. (1988) Oxygen radicals in biology and medicine (Eds. M.G. Simic, K.A. Taylor, J.G. Ward and C. von Sonntag). Plenum Press, New York, 1095 p.
146. Simons A., Ruppert T., Schmidt C., Schlicksupp A., Pipkom R., Reed J., Masters C.L., White A.R., Cappai R., Beyreuther K., Bayer T.A., Multhaup G. (2002) Evidence for a copper-binding superfamily of the amyloid precursor protein. Biochemistry 41: 9310-9320.
147. Smith C.D., Carney J.M., Starke-Reed P.E., Oliver C.N., Stadtman E.R., Floyd R.A., Markesbery W.R. (1991) Excess brain protein oxidation and enzyme dysfunction in normal aging and in Alzheimer disease. Proc Natl Acad Sci USA 88: 10540-10543.
148. Smith C.D., Carney J.M., Tatsumo T., Stadtman E.R., Floyd R.A., Markesbery W.R. (1992) Protein oxidation in aging brain. Ann N Y Acad Sci 663: 110-119.
149. Smith M.A., Harris P.L.R., Sayre L.M., Perry G. (1997) Iron accumulation in Alzheimer disease is a source of redox-generated free radicals. Proc Natl Acad Sci U S A 94: 9866-9868.
150. Smith M.A., Hirai K., Hsiao K., Papolla M.A., Harris P.L.R., Siedlak S.L., Tabaton M., Perry G. (1998) Amyloid-β deposition in Alzheimer transgenic mice is associated with oxidative stress. J Neurochem 70: 2212-2215.
151. Smith M.A., Perry G. (1998) The role of oxidative stress in the pathological sequelae of Alzheimer disease. In: Free radicals, oxidative stress, antioxidants. Pathological and physiological significance (Eds. T. Özben). Plenum Press, New York, p. 195-204.
152. Smith M.A., Perry G., Pryor W.A. (2002) Causes and consequences of oxidative stress in Alzheimer's disease. Free Radic Biol Med 32: 1049.
153. Smith M.A., Rottkamp C.A., Nunomura A., Raina A.K., Perry G. (2000) Oxidative stress in Alzheimer's disease. Biochim Biophys Acta 1502: 139-144.
154. Smith M.A., Sayre L.M., Perry G. (1996) Is Alzheimer's a disease of oxidative stress? Alzheimer's Dis Rev 1: 63-67.
155. Smoluk G.D., Fahey R.C., Ward J.F. (1988) Interaction of glutathione and other low-molecular-weight thiols with DNA: Evidence for counterion condensation and co-ion depletion near DNA. Radiat Res 114: 3-10.
156. Sorimachi K., Craik D.J. (1994) Structure determination of extracellural fragments of amyloid proteins involved in Alzheimer's disease and Duch-type hereditary cerebral haemorrhage with amylosis. Eur J Biochem 219: 237-251.
157. Stadtman E.R. (1990) Metal ion-catalyzed oxidation of proteins: Biochemical mechanism and biological consequences. Free Radic Biol Med 9: 315-325.
158. Stadtman E.R. (1998a) Free radicals mediated oxidation of proteins. In: Free radicals, oxidative stress, and antioxidants. Pathological and physiological significance (Eds. T. Özben). Plenum Press, New York, p. 39-50.
159. Stadtman E.R. (1998b). The role of free radicals mediation of proteins oxidation in aging and disease. In: Free radicals, oxidative stress, and antioxidants. Pathological and physiological significance (Eds. T. Özben). Plenum Press, New York, p. 131-144.
160. Stadtman E.R., Berlett B.S. (1997) Reactive oxygen-mediated protein oxidation in aging and disease. Chem Res Toxicol 10: 485-494.
161. Steffen L.K., Glass R.S., Sabahi M., Wilson G.S., Schöneich C., Mahling S., Asmus K.-D. (1991) OH radical induced decarboxylation of amino acids. Decarboxylation vs. bond formation in radical intermediates. J Am Chem Soc 113: 2141-2145.
162. Sticht H., Bayer P., Willbold D., Dames S., Hilbich C., Beyreuther K., Frank R.W., Rosch P. (1995) Structure of amyloid A4-(1-40)-peptide of Alzheimer's disease. Eur J Biochem 233: 293-298.
163. Stockel J., Safar J., Wallace A.C., Cohen F.E., Prusiner S.B. (1998) Prion protein selectively binds copper(II) ions. Biochemistry 37: 7185-7193.
164. Straub J.E., Guevara J., Huo S., Lee J.P. (2002) Long time dynamic simulations: exploring the folding pathways of an Alzheimer's amyloid Aβ-Peptide. Acc Chem Res 35: 473-481.
165. Stubbe J., van der Donk W. (1998) Protein radicals in enzyme catalysis. Chem Rev 98: 705-762.
166. Tabner B.J., Turnbull S., El Agnaf O.M., Allsop D. (2002) 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 32: 1076-1083.
167. Talafous J., Marcinowski K.J., Klopman G., Zagorski M.G. (1994) Solution structure of residues 1-28 of the amyloid β-peptide. Biochemistry 33: 7788-7796.
168. Tanzi R.E., Bush A.I., Wasco W. (1994) Genetic studies of Alzheimer's disease: lessons learned and future imperatives. Neurobiol Aging Suppl 2: S145-S148.
169. Taylor J.P., Hardy J., Fischbeck K.H. (2002) Toxic proteins in neurodegenerative disease. Science 296: 1991-1995.
170. Terzi E., Hölzemann G., Seelig J. (1995) Self-association of β-amyloid peptide (1-40) in solution and binding to lipid membranes. J Mol Biol 252: 633-642.
171. Terzi E., Hölzemann G., Seelig J. (1997) Interaction of Alzheimer β-amyloid peptide(1-40) with lipid membranes. Biochemistry 36: 14845-14852.
172. Thunecke M., Lobbia A., Kosciessa U., Dyrks T., Oakley A.E., Turner J., Saenger W., Georgalis Y. (1998) Aggregation of Aβ Alzheimer's disease-related peptide studied by dynamic light scattering. J Pept Res 52: 509-517.
173. + with dioxygen; comparison with the Fenton chemistry. Acta Biochim Pol 47: 951-962.
174. Varadarajan S., Kański J., Aksenova M., Lauderback C., Butterfield D.A. (2001) Different mechanisms of oxidative stress and neurotoxicity for alzheimer's Aβ(1-42) and Aβ(25-35). J Am Chem Soc 123: 5625-5631.
175. Varadarajan S., Yatin S., Aksenova M., Butterfield D.A. (2000a) Review: Alzheimer's amyloid β-peptide-associated free radical oxidative stress and neurotoxicity. J Struct Biol 130: 184-208.
176. Varadarajan S., Yatin S., Aksenova M., Butterfield D.A. (2000b) Alzheimer's amyloid β-peptide (1-42) fibrils are not always neurotoxic. Alzheimer's Rep 3: 71-76.
177. Viles J.H., Cohen F.E., Prusiner S.B., Goodin D.B., Wright P.E., Dyson H.J. (1999) Copper binding to the prion protein: structural implications of four identical cooperative binding sites. Proc Natl Acad Sci USA 96: 2042-2047.
178. von Sonntag C. (1987) The chemical basis of radiation biology. Taylor and Francis, London, 515 p.
179. von Sonntag C. (1990) Free-radicals reactions involving thiols and disulphides. In: Sulfur-centered reactive intermediates in chemistry and biology (Eds. C. Chatgilialoglu, and K.-D. Asmus). Plenum Press, New York, p. 359-366.
180. Wardman P. (1995) Reaction of thiyl radicals. In: Biothiols in health and disease (Eds. L. Packer and E. Cadenas). Marcel Dekker Inc., New York, p. 1-19.
181. Wardman P. (1998) Evaluation of the "radical sink" hypothesis from a chemical-kinetic viewpoint. J Radioanal Nucl Chem 232: 23-27.
182. Watson A.A., Fairlie D.P., Craik D.J. (1998) Solution structure of methionine-oxidized amyloid β-peptide (1-40). Does oxidation affect conformational switching? Biochemistry 37: 12700-12706.
183. White A.R., Huang X., Jobling M.F., Barrow C.J., Beyreuther K., Masters C.L., Bush A.I., Cappai R. (2001) Homocysteine potentiates copper- and amyloid β peptide-mediated toxicity in primary neuronal cultures: possible risk factors in the Alzheimer's-type neurodegenerative pathways. J Neurochem 76: 1509-1520.
184. White A.R., Multhaup G., Maher F., Bellingham S., Camakaris J., Zheng H., Bush A.I., Beyreuther K., Masters C.L., Cappai R. (1999b) The Alzheimer's disease amyloid precursor protein modulates copper-induced toxicity and oxidative stress in primary neuronal cultures. J Neurosci 19: 9170-9179.
185. White A.R., Reyes R., Mercer J.F., Camakaris J., Zheng H., Bush A.I., Multhaup G., Beyreuther K., Masters C.L., Cappai R. (1999a) Copper levels are increased in the cerebral cortex and liver of APP and APLP2 knockout mice. Brain Res 842: 439-444.
186. Winyard P.G., Blake D.R., Evans C.H. (2000) Free radicals and inflammation (Eds. P.G. Winyard, D. R. Blake and C.H. Evans). Birkhäuser Verlag, Basel, 259 p.
187. Wong B.S., Wang H., Brown D.R., Jones I.M. (1999) Selective oxidation of methionine residues in prion proteins. Biochem Biophys Res Commun 259: 352-355.
188. Yan S.D., Chen X., Fu J., Chen M., Zhu H., Roher A., Slattery T., Zhao L., Nagashima M., Morser J., Migheli A., Nawroth P., Stem D., Schmidt A.M. (1996) RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease. Nature 382: 685-691.
189. Yankner B.A., Duffy L.K., Kirschner D.A. (1990) Neurotrophic and neurotoxic effects of amyloid-β protein: reversal by tachykinin neuropeptides. Science 250: 279-282.
190. Yokel R.A. (2000) The toxicology of aluminum in the brain: a review. Neurotoxicology 21: 813-828.
191. Yuan J., Yankner B.A. (2000) Apoptosis in the nervous system. Nature 407: 802-809.
192. Zagorski M.G., Barrow C.J. (1992) NMR studies of amyloid β-peptides: Proton assignments, secondary structure, mechanism of an α-helical-β-sheet conversion for a homologous, 28-residue, N-terminal fragment. J Biol Chem 269: 627-632.
193. Zahn R., Liu A., Luhrs T., Riek R., von Schroetter C., Lopez G.F., Billeter M., Calzolai L., Wider G., Wuthrich K. (2000) NMR solution structure of the human prion protein. Proc Natl Acad Sci U S A 97: 145-150.
194. Zappacosta B., Moredente A., Persichilli S., Minucci A., Carlino A., Martorana G.E., Giardina B., De Sole P. (2003) Is homocysteine a pro-oxidant? Free Radic Res 35: 499-505.
195. Zhao F., Ghezzo-Schöneich E., Aced G.I., Hong J., Milby T., Schöneich C. (1997a) Metal-catalyzed oxidation of histidine in human growth hormone. Mechanism, isotope effects, and inhibition by a mild denaturing alcohol. J Biol Chem 272: 9019-9029.
196. Zhao R. (1998) Thiyl radicals, reaction and redox chemistry. Ph.D. Thesis Department of Chemistry. Nuclear Chemistry Royal Institute of Technology, Stockholm, Sweden.
197. Zhao R., Lind J., Merényi G., Eriksen T.E. (1997b) Significance of the intramolecular transformation of glutathione thiyl radicals to a-aminoalkyl radicals. Thermochemical and biological implications. J Chem Soc Perkin Trans 2, p. 569-574.
198. 2 reactions. In: Bioinorganic chemistry of copper (Eds. K.D. Karlin and Z. Tyeklar). Chapman & Hall, p. 264-276.