Interaction of β-amyloid(1-40) peptide with pairs of metal ions: An electrospray ion trap mass spectrometric model study

Biophysical Chemistry

Volumn 144, Issue 1-2, 2009, Pages 9-20

  Drochioiu, Gabi ^a   Manea, Marilena ^b   Dragusanu, Mihaela ^b   Murariu, Manuela ^c   Dragan, Ecaterina Stela ^c   Petre, Brandusa Alina ^b   Mezo, Gabor ^d   Przybylski, Michael ^b  

^a ALEXANDRU IOAN CUZA UNIVERSITY OF IASI   (Romania)

^b UNIVERSITY OF KONSTANZ   (Germany)

^c PETRU PONI INSTITUTE OF MACROMOLECULAR CHEMISTRY   (Romania)

^d EÖTVÖS LORÁND UNIVERSITY   (Hungary)

Author keywords

Alzheimer's disease; Amyloid peptide; ESI ion trap MS; Metal ion peptide complex

Indexed keywords

AMYLOID BETA PROTEIN[1-40]; COPPER; METAL ION; NICKEL; SILVER; ZINC;

ACIDITY; ARTICLE; ATOMIC FORCE MICROSCOPY; BINDING AFFINITY; BINDING KINETICS; CIRCULAR DICHROISM; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ELECTROSPRAY MASS SPECTROMETRY; METAL BINDING; MOLECULAR MODEL; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN BINDING;

AMYLOID BETA-PROTEIN; CIRCULAR DICHROISM; COPPER; HYDROGEN-ION CONCENTRATION; METALS; MICROSCOPY, ATOMIC FORCE; NICKEL; PEPTIDE FRAGMENTS; PROTEIN BINDING; SILVER; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; ZINC;

EID: 67849103574     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2009.05.008     Document Type: Article

References (48)

1. 2+ with histidine-containing peptides. J. Am. Chem. Soc. 117 (1995) 11314-11319
2. Zirah S., Rebuffat S., Kozin S.A., Debey P., Fournier F., Lesage D., and Tabet J.C. Zinc binding properties of the amyloid fragment Abeta(1-16) studied by electrospray-ionization mass spectrometry. Int. J. Mass Spectrom. 228 (2003) 999-1016
3. Adlard P.A., and Bush A.I. Metals and Alzheimer's disease. J. Alzheimer's Dis. 10 (2006) 145-163
4. Bush A.I. The metallobiology of Alzheimer's disease. Trends Neurosci. 26 (2003) 207-214
5. Barnham K.J., Masters C.L., and Bush A.I. Neurodegenerative diseases and oxidative stress. Nat. Rev. Drug Discov. 3 (2004) 205-214
6. Maynard C.J., Bush A.I., Masters C.L., Cappai R., and Li Q.X. Metals and amyloid-beta in Alzheimer's disease. Int. J. Exp. Pathol. 86 (2005) 147-159
7. Smith D.G., Cappai R., and Barnham K.J. The redox chemistry of the Alzheimer's disease amyloid-β peptide. BBA-Biomembranes 1768 (2007) 1976-1990
8. Lahiri D.K., Chen D.M., Lahiri P., Bondy S., and Greig N.H. Amyloid, cholinesterase, melatonin and metals, and their roles in aging and neurodegenerative diseases. Ann. N.Y. Acad. Sci. 1056 (2005) 430-449
9. Scheibe R.J., Kuehl H., Krautwald S., Meissner J.D., and Mueller W.H. Ecto-alkaline phosphatase activity identified at physiological pH range on intact P19 and HL-60 cells is induced by retinoic acid. J. Cell. Biochem. 76 (2000) 420-436
10. Lau T.L., Gehman J.D., Wade J.D., Masters C.L., Barnham K.J., and Separovic F. Cholesterol and clioquinol modulation of Aβ(1-42) interaction with phospholipid bilayers and metals. BBA-Biomembranes 1768 (2007) 3135-3144
11. Atwood C.S., Scarpa R.C., Huang X., Moir R.D., Jones W.D., Fairlie D.P., Tanzi R.E., and Bush A.I. Characterization of copper interactions with Alzheimer amyloid β peptides: identification of an attomolar-affinity copper binding site on amyloid β1-42. J. Neurochem. 75 (2000) 1219-1233
12. Lee J.Y., Cole T.B., Palmiter R.D., Suh S.W., and Koh J.Y. Proc. Contribution by synaptic zinc to the gender-disparate plaque formation in human Swedish mutant APP transgenic mice. Natl. Acad. Sci. U. S. A. 99 (2002) 7705-7710
13. Terry R.D. The pathogenesis of Alzheimer disease: an alternative to the amyloid hypothesis. J. Neuropathol. Exp. Neurol. 55 (1996) 1023-1025
14. Huang X., Atwood C.S., Moir R.D., Hartshorn M.A., Vonsattel J.P., Tanzi R.E., and Bush A.I. Zinc-induced Alzheimer's Abeta(1-42) aggregation is mediated by conformational factors. J. Biol. Chem. 272 (1997) 26464-26470
15. Lovell M.A., Xie C., and Markesbery W.R. Protection against amyloid beta peptide toxicity by zinc. Brain Res. 823 (1999) 88-95
16. Atwood C.S., Moir R.D., Huang X., Scarpa R.C., Bacarra N.M.E., Romano D.M., Hartshorn M.A., Tanzi R.E., and Bush A.I. Dramatic aggregation of Alzheimer A_ by Cu(II) is induced by conditions representing physiological acidosis. J. Biol. Chem. 273 (1998) 12817-12826
17. Drago D., Bettella M., Bolognin S., Cendron L., Scancar J., Milacic R., Ricchelli F., Casini A., Messori L., Tognon G., and Zatta P. Potential pathogenic role of beta-amyloid(1-42)-aluminum complex in Alzheimer's disease. Int. J. Biochem. Cell Biol. 40 (2008) 731-746
18. 2+ binding to amyloid-beta peptide (Aβ) of Alzheimer's disease. BBA-Proteins Proteom 1764 (2006) 246-256
19. Curtain C.C., Ali F., Volitakis I., Cherny R.A., Norton R.S., Beyreuther K., Barrow C.J., Masters C.L., and Bush A.I. K. Alzheimer's disease amyloid-b binds Cu and Zn to generate an allosterically ordered membrane-penetrating structure containing SOD-like subunits. J. J. Biol. Chem. 276 (2001) 20466-20473
20. White A.R., Barnham K.J., Huang X., Voltakis I., Beyreuther K., Masters C.L., Cherny R.A., Bush A.I., and Cappai R. Iron inhibits neurotoxicity induced by trace copper and biological reductants. J. Biol. Inorg. Chem. 9 (2004) 269-280
21. + depletion in neuronal cells. Neurosci. Res. 57 (2007) 454-461
22. Wang S.Z., Chen Y., Sun Z.H., Zhou Q., and Sui S.F. Escherichia coli CorA periplasmic domain functions as a homotetramer to bind substrate. J. Biol. Chem. 281 (2006) 26813-26820
23. Schlosser G., Stefanescu R., Przybylski M., Murariu M., Hudecz F., and Drochioiu G. Copper-induced oligomerization of peptides: a model study. Eur. J. Mass Spectrom. 13 (2007) 331-337
24. Murariu M., Dragan E.S., and Drochioiu G. Synthesis and mass spectrometric characterization of a metal-affinity decapeptide: copper-induced conformational alterations. Biomacromolecules 8 (2007) 3836-3841
25. Popa K., Murariu M., Schlosser G., Molnar R., Cecal A., and Drochioiu G. Effect of radioactive and non-radioactive mercury on wheat germination and the anti-toxic role of glutathione. Isot. Environ. Health Stud. 2 (2007) 105-116
26. Drochioiu G., Damoc E.N., and Przybylski M. Novel UV assay for protein determination and the characterization of copper-protein complexes by mass spectrometry. Talanta 69 (2006) 556-564
27. Drochioiu G., Murariu M., Petre B.A., Manea M., and Przybylski M. Synthesis and characterization of a nonapeptide with specific Cu-binding properties. Rev. Chim. (Bucharest) 58 (2007) 311-315
28. Gradinaru R., Murariu M., Dragan E.S., and Drochioiu G. Protein determination based on the biuret absorbtion in the UV range and copper binding to peptides. Roum. Biotechnol. Lett. 12 (2007) 3235-3239
29. Smith D.P., Smith D.G., Curtain C.C., Boas J.F., Pilbrow J.R., Ciccotosto G.D., Lau T.L., Tew D.J., Perez K., Wade J.D., Bush A.I., Drew S.C., Separovic F., Masters C.L., Cappai R., and Barnham K.J. Copper-mediated amyloid-toxicity is associated with an intermolecular histidine bridge. J. Biol. Chem. 281 (2006) 15145-15154
30. Syme C.D., Nadal R.C., Rigby S.E.J., and Viles J.H. Copper binding to the amyloid-{beta} (a{beta}) peptide associated with Alzheimer's disease: folding, coordination geometry, pH dependence, stoichiometry, and affinity of A{beta}-(1-28): insights from a range of complementary sectroscopic techniques. J. Biol. Chem. 279 (2004) 18169-18177
31. Karr J.W., Akintoye H., Kaupp L.J., and Szalai V.A. N-Terminal deletions modify the Cu2+ binding site in amyloid-β. Biochemistry 44 (2005) 5478-5487
32. Karr J.W., Kaupp L.J., and Szalai V.A. Amyloid-ß binds copper(II) in a mononuclear metal ion binding site. J. Am. Chem. Soc. 126 (2004) 13534-13538
33. Lagadic-Gossmann D., Huc L., and Lecureur V. Alterations of intracellular pH homeostasis in apoptosis: origins and roles. Cell Death Differ. 11 (2004) 953-961
34. Chappell D., Hofmann-Kiefer K., Jacob M., Conzen P., and Rehm M. Metabolic alkalosis despite hyperlactatemia and hypercapnia: interpretation and therapy with help of the Stewart concept. Anaesthesist 57 (2008) 139-142
35. Aoki M., Nomura F., Stromski M.E., Tsuji M.K., Fackler J.C., Hickey P.R., Holtzman D.H., and Jonas R.A. Effects of pH on brain energetics after hypothermic circulatory arrest. Ann. Thorac. Surg. 55 (1993) 1093-1103
36. Yates C.M., Butterworth J., Tennant M.C., and Gordon A. Enzyme activities in relation to pH and lactate in postmortem brain in Alzheimer-type and other dementias. J. Neurochem. 55 (2006) 1624-1630
37. Anderson R.E., and Meyer F.B. Is intracellular brain pH a dependent factor in NOS inhibition during focal cerebral ischemia?. Brain Res. 856 (2000) 220-226
38. Hanson, 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., and Bush A.I. Cu(II) potentiation of Alzheimer Abeta neurotoxicity. Correlation with cell-free hydrogen peroxide production and metal reduction. J. Biol. Chem. 274 (1999) 37111-37116
39. Tickler A.K., Clippingdale A.B., and Wade J.D. Amyloid-b as a 'difficult sequence' in solid phase peptide synthesis. Protein Pept. Lett. 11 (2004) 377-384
40. Antzutkin O.N. Amyloidosis of Alzheimer's Abeta peptides: solid-state nuclear magnetic resonance, electron paramagnetic resonance, transmission electron microscopy, scanning transmission electron microscopy and atomic force microscopy studies. Magn. Reson. Chem. 42 (2004) 231-246
41. Yang D.S., McLaurin J.A., Qin K., Westaway D., and Fraser P.E. Examining the zinc binding site of the amyloid-beta peptide. FEBS J. 267 (2000) 6692-6698
42. Zirah S., Kozin S.A., Mazur A.K., Blond A., Cheminant M., Ségalas-Milazzo I., Debey P., and Rebuffat S. Structural changes of region 1-16 of the Alzheimer disease amyloid beta-peptide upon zinc binding and in vitro aging. J. Biol. Chem. 281 (2006) 2151-2161
43. Ciuculescu E.D., Mekmouche Y., and Faller P. Metal-binding properties of the peptide APP170-188: a model of the ZnII-binding site of amyloid precursor protein (APP). Chem-Eur. J. 11 (2004) 903-909
44. Miura T., Mitani S., Takanashi C., and Mochizuki N. Copper selectively triggers beta-sheet assembly of an N-terminally truncated amyloid beta-peptide beginning with Glu3. J. Inorg. Biochem. 98 (2004) 10-14
45. Jószai V., Nagy N., O{double acute}sz K., Sanna D., Di Natale G., La Mendola D., Pappalardo G., Rizzarelli G., and Sóvágó I. Transition metal complexes of terminally protected peptides containing histidyl residues. J. Inorg. Biochem. 100 (2006) 1399-1409
46. Lau T.L., Barnham J.K., Curtain C.C., Masters C.L., and Separovic F. Magnetic resonance studies of -amyloid peptides. Aust. J. Chem. 56 (2003) 343-348
47. Xu Y., Shen J., Luo X., Zhu W., Chen K., Ma J., and Jiang H. Conformational transition of amyloid {beta}-peptide. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 5403-5407
48. Klug G.M., Losic D., Subasinghe S.S., Aguilar M.I., Martin L.L., and Small D.H. Beta-amyloid protein oligomers induced by metal ions and acid pH are distinct from those generated by slow spontaneous ageing at neutral pH. Eur. J. Biochem. 270 (2003) 4282-4293