PH-dependence of the specific binding of Cu(II) and Zn(II) ions to the amyloid-β peptide

Biochemical and Biophysical Research Communications

Volumn 421, Issue 3, 2012, Pages 554-560

  Ghalebani, Leila ^a,b   Wahlström, Anna ^a   Danielsson, Jens ^a   Wärmländer, Sebastian K T S ^a   Gräslund, Astrid ^a  

^a STOCKHOLM UNIVERSITY   (Sweden)

^b KAROLINSKA INSTITUTE   (Sweden)

Author keywords

Alzheimer's disease; Amyloid peptide; Copper and zinc; Metal binding; Metal ions; NMR spectroscopy

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; CUPRIC ION; HISTIDINE; ZINC ION;

ACIDOSIS; ALZHEIMER DISEASE; ARTICLE; BINDING AFFINITY; BINDING SITE; CARBON NUCLEAR MAGNETIC RESONANCE; HETERONUCLEAR SINGLE QUANTUM COHERENCE; IN VIVO STUDY; LIGAND BINDING; METAL BINDING; NITROGEN NUCLEAR MAGNETIC RESONANCE; OXIDATION REDUCTION REACTION; PH; PRIORITY JOURNAL; PROTON NUCLEAR MAGNETIC RESONANCE;

ACIDOSIS; AMYLOID BETA-PEPTIDES; CATIONS, DIVALENT; COPPER; HUMANS; HYDROGEN-ION CONCENTRATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OXIDATION-REDUCTION; PEPTIDE FRAGMENTS; ZINC;

EID: 84860660568     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.04.043     Document Type: Article

References (25)

1. Atwood C.S., Moir R.D., Huang X., Scarpa R.C., Bacarra N.M.E., Romano D.M., Hartshorn M.A., Tanzi R.E., Bush A.I. Dramatic aggregation of Alzheimer Aβ by Cu(II) is induced by conditions representing physiological acidosis. J. Biol. Chem. 1998, 273:12817-12826.
2. 2+ ions accelerate the kinetics of fiber formation and promote cell toxicity of amyloid-β from Alzheimer disease. J. Biol. Chem. 2010, 285:41533-41540.
3. Pedersen J.T., Østergaard J., Rozlosnik N., Gammelgaard B., Heegaard N.H.H. Cu(II) mediates kinetically distinct, non-amyloidogenic aggregation of amyloid-β peptides. J. Biol. Chem. 2011, 286:26952-26963.
4. Miller Y., Ma B., Nussinov R. Zinc ions promote Alzheimer Aβ aggregation via population shift of polymorphic states. Proc. Natl. Acad. Sci. 2010, 107:9490-9495.
5. Tõugu V., Tiiman A., Palumaa P. Interactions of Zn(II) and Cu(II) ions with Alzheimer's amyloid-beta peptide, metal ion binding, contribution to fibrillization and toxicity. Metallomics 2011, 3:250-261.
6. Choi J.-S., Braymer J.J., Nanga R.P.R., Ramamoorthy A., Lim M.H. Design of small molecules that target metal-Aβ species and regulate metal-induced Aβ aggregation and neurotoxicity. Proc. Natl. Acad. Sci. 2010, 107:21990-21995.
7. Hegde M.L., Bharati P., Suram A., Venugopal C., Jagannathan R., Poddar P., Srinivas P., Sambamurti K., Rao K.J., Scancar J., Messori L., Zecca L., Zatta P. Challenges associated with metal chelation therapy in Alzheimer's disease. J. Alzheimers Dis. 2009, 17:457-468.
8. Faller P., Hureau C. Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-β peptide. Dalton Trans. 2009, 38:1080-1094.
9. Faller P. Copper and zinc binding to amyloid-β: coordination, dynamics, aggregation, reactivity and metal-ion transfer. Chembiochem 2009, 10:2837-2845.
10. Danielsson J., Pierattelli R., Banci L., Gräslund A. High-resolution NMR studies of the zinc-binding site of the Alzheimer's amyloid β-peptide. FEBS J. 2007, 274:46-59.
11. Rezaei-Ghaleh N., Giller K., Becker S., Zweckstetter M. Effect of zinc binding on β-amyloid structure and dynamics: implications for Aβ aggregation. Biophys. J. 2011, 101:1202-1211.
12. Rózga M., Kłoniecki M., Dadlez M., Bal W. A direct determination of the dissociation constant for the Cu(II) complex of amyloid β 1-40 peptide. Chem. Res. Toxicol. 2010, 23:336-340.
13. 2+) coordination with beta-amyloid peptide: DFT computational study. Interdiscip. Sci. Comput. Life Sci. 2010, 2:57-69.
14. Lin C.J., Huang H.C., Jiang Z.F. Cu(II) interaction with amyloid-β peptide: a review of neuroactive mechanisms in AD brains. Brain Res. Bull. 2010, 82:235-242.
15. Jarvet J., Danielsson J., Damberg P., Oleszczuk M., Gräslund A. Positioning of the Alzheimer Aβ(1-40) peptide in SDS micelles using NMR and paramagnetic probes. J. Biomol. NMR 2007, 39:63-72.
16. Fezoui Y., Hartley D.M., Harper J.D., Khurana R., Walsh D.M., Condron M.M., Selkoe D.J., Lansbury P.T.J., Fink A.L., Teplow D.B. An improved method of preparing the amyloid β-protein for fibrillogenesis and neurotoxicity experiments. Amyloid 2000, 7:166-178.
17. Delaglio F., Grzesiek S., Vuister G.W., Zhu G., Pfeifer J., Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 1995, 6:277-293.
18. T.D. Goddard, D.G. Kneller, SPARKY 3, University of California, San Francisco.
19. 15N relaxation study of the amyloid β-peptide: structural propensities and persistence length. Magn. Reson. Chem. 2006, 44:S114-S121.
20. M.G. Zagorski, Personal communication by fax, August 06 2004.
21. Fawzi N.L., Ying J., Torchia D.A., Clore G.M. Kinetics of amyloid β monomer-to-oligomer exchange by NMR relaxation. J. Am. Chem. Soc. 2010, 132:9948-9951.
22. Bodner C.R., Dobson C.M., Bax A. Multiple tight phospholipid-binding modes of α-synuclein revealed by solution NMR spectroscopy. J. Mol. Biol. 2009, 390:775-790.
23. Syme C.D., Nadal R.C., Rigby S.E.J., Viles J.H. Copper binding to the amyloid-β (Aβ) peptide associated with Alzheimer's disease. J. Biol. Chem. 2004, 279:18169-18177.
24. Benilova I., Karran E., De Strooper B. The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes. Nat. Neurosci. 2012, 15:1-9.
25. Lovell M.A., Robertson J.D., Teesdale W.J., Campbell J.L., Markesbery W.R. Copper, iron and zinc in Alzheimer's disease senile plaques. J. Neurol. Sci. 1998, 158:47-52.