Alzheimer's disease: Soluble oligomeric Aβ(1-40) peptide in membrane mimic environment from solution NMR and circular dichroism studies

Neurochemical Research

Volumn 29, Issue 12, 2004, Pages 2267-2272

  Mandal, Pravat K ^a   Pettegrew, Jay W ^a  

^a Pennsylvania State Univ Univ P   (United States)

Author keywords

A peptide; Alzheimer's disease; CD; micelle; NMR; oligomer

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; MONOMER; OLIGOMER;

ALPHA HELIX; ALZHEIMER DISEASE; ARTICLE; BRAIN; CIRCULAR DICHROISM; MEMBRANE STRUCTURE; MOLECULAR MIMICRY; NEUROTOXICITY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN CONFORMATION; SENILE PLAQUE;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; AMYLOID BETA-PROTEIN; CELL MEMBRANE; CIRCULAR DICHROISM; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MEMBRANES; MOLECULAR SEQUENCE DATA; NEURONS; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY; SOLUTIONS;

EID: 11144326857     PISSN: 03643190     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11064-004-7035-1     Document Type: Article

References (38)

1. Rochet, J. C. and Lansbury, P. T., Jr. 2000. Amyloid fibrillogenesis: Themes and variations. Curr. Opin. Struct. Biol. 10:60-68.
2. Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., Wals, P., Zhang, C., Finch, C. E., Krafft, G. A. and Klein, W. L. 1998. Diffusible, nonfibrillar ligands derived from Abetal-42 are potent central nervous system neurotoxins. Proc. Natl. Acad. Sci. USA 95:6448-6453.
3. Kuo, Y. M., Emmerling, M. R., Vigo-Pelfrey, C., Kasunic, T. C., Kirkpatrick, J. B., Murdoch, G. H., Ball, M. J., and Roher, A. E. 1996. Water-soluble A beta (N-40, N-42) oligomers in normal and Alzheimer disease brains. J. Biol. Chem. 271:4077-4081.
4. Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., and Glabe, C. G. 2003. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300:486-489.
5. Dahlgren, K. N., Manelli, A. M., Stine, W. B., Baker, L. K., Krafft, G. A., and LaDu, M. J. 2002. Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability. J. Biol. Chem. 277:32046-32053.
6. Rodrigues, C. M., Sola, S., Brito, M. A., Brondino, C. D., Brites, D. and Moura, J. J. 2001. Amyloid beta-peptide disrupts mitochondrial membrane lipid and protein structure: Protective role of tauroursodeoxycholate. Biochem. Biophys. Res. Commun. 281:468-474.
7. Mason, R. P., Jacob, R. F., Walter, M. F., Mason, P. E., Avdulov, N. A., Chochina, S. V., Igbavboa, U., and Wood, W. G. 1999. Distribution and fluidizing action of soluble and aggregated amyloid beta-peptide in rat synaptic plasma membranes. J. Biol. Chem. 274:18801-18807.
8. Mason, R. P., Trumbore, M. W., and Pettegrew, J. W. 1996. Molecular membrane interactions of a phospholipid metabolite - Implications for Alzheimer's disease pathophysiology. Neurobiol. Alzheimer Dis. 777:368-373.
9. Pettegrew, J. W., Withers, G., Panchalingam, K., and Post, J. F. 1987. 31P nuclear magnetic resonance (NMR) spectroscopy of brain in aging and Alzheimer's disease. J. Neural. Transm. Suppl. 24:261-268.
10. 31P nuclear magnetic resonance studies of phosphoglyceride metabolism in developing and degenerating brain: Preliminary observations. J. Neuropathol Exp. Neurol. 46:419-430.
11. 31P nuclear magnetic resonance study of the brain in Alzheimer's disease. J Neuropathol. Exp. Neurol. 47:235-248.
12. Pettegrew, J. W., Panchalingam, K., Moossy, J., Martinez, J., Rao, G., and Boller, F. 1988. Correlation of phosphorus-31 magnetic resonance spectroscopy and morphologic findings in Alzheimer's disease. Arch. Neurol. 45:1093-1096.
13. Pettegrew, J. W. 1989. Molecular insights into Alzheimer's disease. Ann. N Y Acad. Sci. 568:5-28.
14. Pettegrew, J. W., Panchalingam, K., Hamilton, R. L., and McClure, R. J. 2001. Brain membrane phospholipid alterations in Alzheimer's disease. Neurochem. Res. 26:771-782.
15. Pettegrew, J. W., Panchalingam, K., Stanley, J. A., and McClure, R. J. 2002. P-31 and H-1 MRSI studies of psychosis in Alzheimer's disease. Am. J. Geriatr. Psychiatry. 10: 18-19.
16. Dante, S., Hauss, T., and Dencher, N. A. 2002. Beta-amyloid 25 to 35 is intercalated in anionic and zwitterionic lipid membranes to different extents. Biophys. J. 83:2610-2616.
17. Bokvist, M., Lindstrom, F., Watts, A., and Grobner, G. 2004. Two types of Alzheimer's beta-amyloid (1-40) peptide membrane interactions: Aggregation preventing transmembrane anchoring versus accelerated surface fibril formation. J. Mol. Biol. 335:1039-1049.
18. Terzi, E., Holzemann, G., and Seelig, J. 1997. Interaction of Alzheimer beta-amyloid peptide(1-40) with lipid membranes. Biochemistry 36:14845-14852.
19. Pettegrew, J. W., Panchalingam, K., Withers, G., McKeag, D., and Strychor, S. 1990. Changes in brain energy and phospholipid metabolism during development and aging in the Fischer 344 rat. J. Neurobiol. Exp. Neuropathol. 49:237-249.
20. Geddes, J. W., Panchalingam, K., Keller, J. N., and Pettegrew, J. W. 1997. Elevated phosphocholine and phosphatidylcholine following rat entorhinal cortex lesions. Neurobiol. Aging 18:305-308.
21. Tieleman, D. P., van der Spoel, D. and Berendsen, H. J. C. 2000. Molecular dynamics simulations of dodecylphosphocholine micelles at three different aggregate sizes: Micellar structure and chain relaxation. J. Phys. Chem. B 104:6380-6388.
22. Lauterwein, J., Bosch, C., Brown, L. R., and Wuthrich, K. 1979. Physicochemical studies of the protein-lipid interactions in melittin-containing micelles. Biochim. Biophys. Acta. 566:243-246.
23. Wallace, B. A., Janes, R. W., and Orry, A. 2001. Secondary structure information content on the VUV region of synchrotron radiation circular dichroism (SRCD) spectra. Biophys. J. 80:28a.
24. Lobley, A. and Wallace, B. A. 2001. Dichroweb: A website for the analysis of protein secondary structure from circular dichroism spectra. Biophys. J. 80:373a.
25. Mandal, P. K. and Majumdar, A. 2004. A comprehensive discussion of HSQC and HMQC pulse sequences. Concepts Magn. Reson. Part A 20A:1-23.
26. Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995). NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6:277-293.
27. Garrett, D. S., Powers, R., Gronenborn, A. M., and Clore, G. M. 1991. A common sense approach to peak picking two-, three- and four-dimensional spectra using automatic computer analysis of contour diagrams. J. Magn. Reson. 95: 214-220.
28. Goddard, T. D., and Kneller, D. G. 1994. SPARKY 3, University of California, San Francisco.
29. Chandra, S., Chen, X. C., Rizo, J., Jahn, R., and Sudhof, T. C. 2003. A broken alpha-helix in folded alpha-synuclein. J. Biol. Chem. 278:15313-15318.
30. Mandal, P. K. 2002. Complete NMR spectroscopic assignment of a neuronal transduction protein. Monatsh. Chem.133:205-217.
31. Mandal, P. K. and Pettegrew, J. W. 2004. Alzheimer's disease: NMR studies of asialo (GM1) and trisialo (GT1b) ganglioside interactions with A beta(1-40) peptide in a membrane mimic environment. Neurochem. Res. 29:447-453.
32. Pervushin, K., Riek, R., Wider, G., and Wuthrich, K. 1997. Attenuated T-2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc. Natl. Acad. Sci. USA 94:12366-12371.
33. Wuthrich, K. 1986. NMR of Proteins and Nucleic Acids. John Wiley and Sons, Inc. New York.
34. Schwieters, C. D., Kuszewski, J. J., Tjandra, N., and Clore, G. M. 2003. The Xplor-NIH NMR molecular structure determination package. J. Magn. Reson. 160:65-73.
35. Marcinowski, K. J., Shao, H., Clancy, E. L., and Zagorski, M. G. 1998. Solution structure model of residues 1-28 of the amyloid beta peptide when bound to micelles. J. Am. Chem. Soc. 120:11082-11091.
36. Lashuel, H. A., Hartley, D., Petre, B. M., Walz, T., and Lansbury, P. T., Jr. 2002. Neurodegenerative disease: Amyloid pores from pathogenic mutations. Nature 418:291.
37. Hartley, D. M., Walsh, D. M., Ye, C. P., Diehl, T., Vasquez, S., Vassilev, P. M., Teplow, D. B. and Selkoe, D. J. 1999. Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. J. Neurosci. 19:8876-8884.
38. Mandal, P. K. and Pettegrew, J. W. 2004. Structure and dynamics studies of ganglioside-Ab peptide in Alzheimer's disease. Biophys. J. 86:340.