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Spatial structure of beta-amyloid Aβ1-40 in complex with a biological membrane model

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DOI: 10.4236/aad.2012.13004    3,673 Downloads   7,444 Views   Citations

ABSTRACT

The spatial structure of beta-amyloid Aβ1-40 in complex with sodium dodecyl sulfate micelles as a model membrane system was investigated by 1H-1H two-dimensional NMR (TOCSY, NOESY) spectroscopy and molecular dynamic method calculations. On the basis of NOE and chemical shifts changes data, spatial structure of the complex beta-amyloid-model of the cell surface membrane was obtained.

Conflicts of Interest

The authors declare no conflicts of interest.

Cite this paper

Usachev, K., Filippov, A., Antzutkin, O. and Klochkov, V. (2012) Spatial structure of beta-amyloid Aβ1-40 in complex with a biological membrane model. Advances in Alzheimer's Disease, 1, 22-29. doi: 10.4236/aad.2012.13004.

References

[1] Coles, M., Bicknell, W., Watson, A., Fairlie, D.P. and Craik, D.J. (1998) Solution structure of amyloid β-peptide (1-40) in a water-micelle enviroment. Is the membrane- spanning domain where we think it is? Biochemistry, 37, 11064-11077. doi: 10.1021/bi972979f
[2] Dahlgren, K.L., Manelli, A.M., Stine, W.B., Baker, L.K., Krafft, G.A. and LaDu, M.J. (2004) Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability. Journal of Biological Chemistry, 277, 32046-32053. doi: 10.1074/jbc.M201750200
[3] Lansbury, P.T. (1999) Evolution of amyloid: What normal protein folding may tell us about fibrillogenesis and disease. Proceedings of National Academy Sciences of the USA, 96, 3342-3344. doi: 10.1073/pnas.96.7.3342
[4] Lansbury, P.T. (2002) Neurodegenerative disease: Amyloid pores from pathogenic mutations. Nature, 418, 291. doi: 10.1038/418291a
[5] Petkova, A.T., Leapman, R.D., Guo, Z.H., Yau, W.M., Mattson, M.P. and Tycko, R. (2005) Self-propagating, molecular-level polymorphism in Alzheimer’s β-amyloid fibrils. Science, 307, 262-265. doi: 10.1126/science.1105850
[6] Selkoe, D.J. (1995) Deciphering Alzheimer’s disease: Molecular genetics and cell biology yield major clues. Journal of National Institutes of Health, 7, 57-64.
[7] Walsh, D.M., Klyubin, I., Fadeeva, J.V., Cullen, W.K., Anwyl, R., Wolfe, M.S., Rowan, M.J. and Selkoe, D.J. (2002) Naturally secreted oligomers of amyloid protein potently inhibit hippocampal long-term potentiation in vivo. Nature, 416, 535-539. doi: 10.1038/416535a
[8] Aisenbrey, C., Borowik, T., Bystrom, R., Bokvist, M., Lindstrom, F., Misiak, H., Sani, M.A. and Grobner, G. (2008) How is protein aggregation in amyloidogenic diseases modulated by biological membranes? European Biophysics Journal, 37, 247-255. doi: 10.1007/s00249-007-0237-0
[9] Gehman, J., O’Brien, C., Shabanpoor, F., Wade, J. and Separovic, F. (2008) Metal effects on the membrane interactions of amyloid-β peptides. European Biophysics Journal, 37, 333-344. doi: 10.1007/s00249-007-0251-2
[10] Jones, J. (2002) Amino acid and peptide synthesis. Oxford University Press, New York, 92.
[11] Filippov, A. (2010) Synthesis and aggregation studies on amyloid oligomers of Alzheimer’s abeta peptides. Lulea University of Technology, Lulea, 26.
[12] Merrifield, R.B. (1963) Solid phase peptide synthesis. I. The synthesis of a tetrapeptide. Journal of the American Chemical Society, 85, 2149-2154. doi: 10.1021/ja00897a025
[13] Wuthrich, K. (1986) NMR of proteins and nucleic acids. Wiley-VCH, New York, 1-292.
[14] Blokhin, D.S., Efimov, S.V., Klochkov, A.V., Yulmetov, A.R., Filippov, A.V., Antzutkin, O.N., Aganov, A.V. and Klochkov, V.V. (2011) Spatial structure of the decapeptide Val-Ile-Lys-Lys-Ser-Thr-Ala-Leu-Leu-Gly in water and in a complex with sodium dodecyl sulfate micelles. Applied Magnetic Resonance, 41, 267-282. doi: 10.1007/s00723-011-0257-x
[15] Schwieters, C.D., Kuszewski, J.J., Tjandra, N. and Clore, G.M. (2003) The Xplor-NIH NMR molecular structure determination package. Journal of Magnetic Resonance, 160, 65-73. doi: 10.1016/S1090-7807(02)00014-9
[16] Smith, R., Separovic, F., Milne, T.J., Whittaker, A., Bennett, F.M., Cornell, B.A. and Makriyannis, A. (1994) Structure and orientation of the pore-forming peptide melittin, in lipid bilayers. Journal of Molecular Biology, 241, 456-466. doi: 10.1006/jmbi.1994.1520
[17] Henry, G.D. and Sykes, B.D. (1994) Methods to study membrane protein structure in solution. Method in Enzimology, 239, 515-535. doi: 10.1016/S0076-6879(94)39020-7
[18] Lee, K.H., Fitton, J.E. and Wüthrich, K. (1987) Nuclear magnetic resonance investigation of the conformation of δ-haemolysin bound to dodecylphosphocholine micelles. Biochimica et Biophysica Acta (BBA)—Protein Structure and Molecular Enzymology, 911, 144-153. doi: 10.1016/0167-4838(87)90003-3
[19] Motta, A., Pastore, A., Goud, N.A. and Castiglione Morelli, M.A. (1991) Solution conformation of salmon calcitonin in sodium dodecyl sulfate micelles as determined by two-dimensional NMR and distance geometry calculations. Biochemistry, 30, 10444-10450. doi: 10.1021/bi00107a012
[20] Wang, G., Keifer, P. and Peterkofsky, A. (2003) Solution structure of the N-terminal amphitropic domain of Escherichia coli glucose-specific enzyme IIA in membrane-mimetic micelles. Protein Science, 12, 1087-1096. doi: 10.1110/ps.0301503
[21] Marcotte, I. and Auger, M. (2005) Bicelles as model membranes for solid- and solution-state NMR studies of membrane peptides and proteins. Concepts in Magnetic Resonance Part A, 24A, 17-37. doi: 10.1002/cmr.a.20025
[22] Ernst, R.R., Bodenhausen, B. and Wokaun, A. (1987) Principles of nuclear magnetic resonance in one and two dimensions. Oxford University Press, Oxford, 610.
[23] Berger, S. and Braun, S. (2004) 200 and more NMR experiments. Wiley-VCH, Weinheim, 810.
[24] Jarvet, J., Danielsson, J., Damberg, P., Oleszczuk, M. and Graslund, A. (2007) Positioning of the Alzheimer Aβ(1-40) peptide in SDS micelles using NMR and paramagnetic probes. Journal of Biomolecular NMR, 39, 63-72. doi: 10.1007/s10858-007-9176-4
[25] Vivekanandan, V., Brender, J.R., Lee, Sh.Y. and Ramamoorthy, A. (2011) A partially folded structure of amyloid-beta(1-40) in an aqueous environment. Biochemical and Biophysical Research Communications, 411, 312-316. doi: 10.1016/j.bbrc.2011.06.133
[26] Usachev, K.S., Efimov, S.V., Yulmetov, A.R., Filippov, A.V., Antzutkin, O.N., Afonin, S. and Klochkov, V.V. (2012) Spatial structure of heptapeptide Abetha(16-22) (beta- amyloid Abetha(1-40) active fragment) in solution and in complex with a biological membrane model. Magnetic Resonance in Chemistry, 50, 784-792. doi: 10.1002/mrc.3880H.

  
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