Mechanism of amyloid β-protein dimerization determined using single-molecule afm force spectroscopy

Scientific Reports

Volumn 3, Issue , 2013, Pages

  Lv, Zhengjian ^a   Roychaudhuri, Robin ^b   Condron, Margaret M ^b   Teplow, David B ^b,c   Lyubchenko, Yuri L ^a  

^a UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

^b Department of Neurology ^*  (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN;

ARTICLE; ATOMIC FORCE MICROSCOPY; CHEMISTRY; HUMAN; PROTEIN FOLDING; PROTEIN MULTIMERIZATION;

AMYLOID BETA-PEPTIDES; HUMANS; MICROSCOPY, ATOMIC FORCE; PROTEIN FOLDING; PROTEIN MULTIMERIZATION;

EID: 84885361410     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep02880     Document Type: Article

References (34)

1. Chiti, F. & Dobson, C. M. Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75, 333-366 (2006). (Pubitemid 44118036)
2. Roychaudhuri, R., Yang, M., Hoshi, M. M. & Teplow, D. B. Amyloid beta-protein assembly and Alzheimer disease. J Biol Chem 284, 4749-4753 (2009).
3. Benilova, I., Karran, E. & De Strooper, B. The toxic Abeta oligomer and Alzheimer's disease: an emperor in need of clothes. Nat Neurosci 15, 349-357 (2012).
4. De Strooper, B., Vassar, R. & Golde, T. The secretases: enzymes with therapeutic potential in Alzheimer disease. Nat Rev Neurol 6, 99-107 (2010).
5. Karran, E., Mercken, M. & De Strooper, B. The amyloid cascade hypothesis for Alzheimer's disease: an appraisal for the development of therapeutics. Nat Rev Drug Discov 10, 698-712 (2011).
6. Pauwels, K. et al. Structural basis for increased toxicity of pathological abeta42:abeta40 ratios in Alzheimer disease. J Biol Chem 287, 5650-5660 (2012).
7. Bitan, G. et al. Amyloid beta-protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways. Proc Natl Acad Sci USA 100, 330-335 (2003).
8. Bernstein, S. L. et al. Amyloid-beta protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease. Nat Chem 1, 326-331 (2009).
9. Yang, M. & Teplow, D. B. Amyloid beta-protein monomer folding: freeenergy surfaces reveal alloform-specific differences. J Mol Biol 384, 450-464 (2008).
10. Roychaudhuri, R. et al. C-terminal turn stability determines assembly differences between Abeta40 and Abeta42. J Mol Biol 425, 292-308 (2013).
11. Yu, J., Warnke, J. & Lyubchenko, Y. L. Nanoprobing of alpha-synuclein misfolding and aggregation with atomic force microscopy. Nanomedicine 7, 146-152 (2011).
12. Kim, B. H. et al. Single-molecule atomic force microscopy force spectroscopy study of Abeta-40 interactions. Biochemistry 50, 5154-5162 (2011).
13. Krasnoslobodtsev, A. V. et al. Effect of spermidine on misfolding and interactions of alpha-synuclein. PLoS One 7, e38099 (2012).
14. Lv, Z., Condron, M. M., Teplow, D. B. & Lyubchenko, Y. L. Nanoprobing of the Effect of Cu(21) Cations on Misfolding, Interaction and Aggregation of Amyloid beta Peptide. J Neuroimmune Pharmacol 8, 262-273 (2013).
15. Portillo, A. M., Krasnoslobodtsev, A. V. & Lyubchenko, Y. L. Effect of electrostatics on aggregation of prion protein Sup35 peptide. J Phys Condens Matter 24, 164205 (2012).
16. Lyubchenko, Y. L., Kim, B. H., Krasnoslobodtsev, A. V. & Yu, J. Nanoimaging for protein misfolding diseases. Wiley Interdiscip Rev Nanomed Nanobiotechnol 2, 526-543 (2010).
17. Lovas, S., Zhang, Y., Yu, J. & Lyubchenko, Y. L. Molecular mechanism of misfolding and aggregation of abeta(13-23). J Phys Chem B 117, 6175-6186 (2013).
18. Petkova, A. T. et al. A structural model for Alzheimer's beta-amyloid fibrils based on experimental constraints from solid state NMR. Proc Natl Acad Sci USA 99, 16742-16747 (2002). (Pubitemid 36034043)
19. Luhrs, T. et al. 3D structure of Alzheimer's amyloid-beta(1-42) fibrils. Proc Natl Acad Sci USA 102, 17342-17347 (2005).
20. Krasnoslobodtsev, A. V., Shlyakhtenko, L. S. & Lyubchenko, Y. L. Probing Interactions within the synaptic DNA-SfiI complex by AFM force spectroscopy. J Mol Biol 365, 1407-1416 (2007). (Pubitemid 46048826)
21. Merkel, R., Nassoy, P., Leung, A., Ritchie, K. & Evans, E. Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy. Nature 397, 50-53 (1999). (Pubitemid 29038244)
22. Mitternacht, S., Staneva, I., Hard, T. & Irback, A. Monte Carlo study of the formation and conformational properties of dimers of Abeta42 variants. J Mol Biol 410, 357-367 (2011).
23. Zhu X., Bora, R. P., Barman, A., Singh, R. & Prabhakar, R. Dimerization of the full-length Alzheimer amyloid beta-peptide (Abeta42) in explicit aqueous solution: a molecular dynamics study. J Phys Chem B 116, 4405-4416 (2012)
24. Barz, B. & Urbanc, B. Dimer formation enhances structural differences between amyloid beta-protein (1-40) and (1-42): an explicit-solvent molecular dynamics study. PLoS One 7, e34345 (2012).
25. Melquiond, A., Dong, X., Mousseau, N. & Derreumaux, P. Role of the region 23-28 in Abeta fibril formation: insights from simulations of the monomers and dimers of Alzheimer's peptides Abeta40 and Abeta42. Curr Alzheimer Res 5, 244-250 (2008). (Pubitemid 351840276)
26. Cote, S., Laghaei, R., Derreumaux, P. & Mousseau, N. Distinct dimerization for various alloforms of the amyloid-beta protein: Abeta(1-40), Abeta(1-42), and Abeta(1-40)(D23N). J Phys Chem B 116, 4043-4055 (2012).
27. Walsh, D. M. & Teplow, D. B. Alzheimer's disease and the amyloid beta-protein. Prog Mol Biol Transl Sci 107, 101-124 (2012).
28. Oesterhelt, F., Rief, M. & Gaub, H. E. Single molecule force spectroscopy by AFM indicates helical structure of poly(ethylene-glycol) in water. New Journal of Physics 1, 6 (1999).
29. Sarkar, A., Caamano, S. & Fernandez, J. M. The elasticity of individual titin PEVK exons measured by single molecule atomic force microscopy. J Biol Chem 280, 6261-6264 (2005). (Pubitemid 40341171)
30. Zhao, J. M. et al. Single-molecule detection of structural changes during Per-Arnt-Sim (PAS) domain activation. Proc Natl Acad Sci USA 103, 11561-11566 (2006). (Pubitemid 44182491)
31. Gu, L., Liu, C. & Guo, Z. Structural insights into Abeta42 oligomers using sitedirected spin labeling. J Biol Chem 288, 18673-18683 (2013).
32. Ball, K. A., Phillips, A. H.,Wemmer, D. E.& Head-Gordon, T. Differences in betastrand Populations of Monomeric Abeta40 and Abeta42. Biophys J 104, 2714-2724 (2013).
33. Maji, S. K. et al. Amino acid position-specific contributions to amyloid betaprotein oligomerization. J Biol Chem 284, 23580-23591 (2009).
34. Tinoco Jr, I. & Bustamante, C. The effect of force on thermodynamics and kinetics of single molecule reactions. Biophys Chem 101-102, 513-533 (2002). (Pubitemid 35462069)