Preparation of pure populations of covalently stabilized amyloid β-protein oligomers of specific sizes

Analytical Biochemistry

Volumn 518, Issue , 2017, Pages 78-85

  Hayden, Eric Y ^a   Conovaloff, Joseph L ^a   Mason, Ashley ^a   Bitan, Gal ^a   Teplow, David B ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Alzheimer's disease; Amyloid protein; Isolation; Oligomers; Protein function; Protein structure

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; DIMETHYL SULFOXIDE; OLIGOMER; UREA; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA-PROTEIN (1-42); PEPTIDE FRAGMENT;

ANIMAL CELL; ARTICLE; BIOLOGICAL ACTIVITY; CONTROLLED STUDY; DENATURATION; DISSOCIATION; FRACTIONATION; MOLECULAR SIZE; MOLECULAR STABILITY; MOLECULAR WEIGHT; NEUROTOXICITY; NONHUMAN; OLIGOMERIZATION; PC12 CELL LINE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN CROSS LINKING; RAT; STRUCTURE ACTIVITY RELATION; CHEMISTRY; HUMAN; ISOLATION AND PURIFICATION;

AMYLOID BETA-PEPTIDES; HUMANS; PEPTIDE FRAGMENTS;

EID: 84995912064     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2016.10.026     Document Type: Article

References (31)

1. [1] Musiek, E.S., Holtzman, D.M., Three dimensions of the amyloid hypothesis: time, space and ‘wingmen’. Nat. Neurosci. 18 (2015), 800–806.
2. [2] Fraser, P.E., Nguyen, J.T., Inouye, H., Surewicz, W.K., Selkoe, D.J., Podlisny, M.B., Kirschner, D.A., Fibril formation by primate, rodent, and Dutch-hemorrhagic analogues of Alzheimer amyloid β-protein. Biochemistry 31 (1992), 10716–10723.
3. [3] Walsh, D.M., Lomakin, A., Benedek, G.B., Condron, M.M., Teplow, D.B., Amyloid β-protein fibrillogenesis. Detection of a protofibrillar intermediate. J. Biol. Chem. 272 (1997), 22364–22372.
4. [4] Harper, J.D., Lieber, C.M., Lansbury, P.T. Jr., Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β protein. Chem. Biol. 4 (1997), 951–959.
5. [5] Harper, J.D., Wong, S.S., Lieber, C.M., Lansbury, P.T., Observation of metastable Aβ amyloid protofibrils by atomic force microscopy. Chem. Biol. 4 (1997), 119–125.
6. [6] Lashuel, H.A., Hartley, D., Petre, B.M., Walz, T., Lansbury, P.T. Jr., Neurodegenerative disease: amyloid pores from pathogenic mutations. Nature, 418, 2002, 291.
7. [7] Xia, W., Zhang, J., Kholodenko, D., Citron, M., Podlisny, M.B., Teplow, D.B., Haass, C., Seubert, P., Koo, E.H., Selkoe, D.J., Enhanced production and oligomerization of the 42-residue amyloid β-protein by Chinese hamster ovary cells stably expressing mutant presenilins. J. Biol. Chem. 272 (1997), 7977–7982.
8. [8] Roychaudhuri, R., Yang, M., Hoshi, M.M., Teplow, D.B., Amyloid β-protein assembly and Alzheimer disease. J. Biol. Chem. 284 (2009), 4749–4753.
9. [9] Bitan, G., Kirkitadze, M.D., Lomakin, A., Vollers, S.S., Benedek, G.B., Teplow, D.B., Amyloid β -protein (Aβ) assembly: Aβ 40 and Aβ 42 oligomerize through distinct pathways. Proc. Natl. Acad. Sci. U. S. A. 100 (2003), 330–335.
10. [10] Walsh, D.M., Klyubin, I., Fadeeva, J.V., Cullen, W.K., Anwyl, R., Wolfe, M.S., Rowan, M.J., Selkoe, D.J., Naturally secreted oligomers of amyloid β-protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416 (2002), 535–539.
11. [11] Gong, Y., Meyer, E.M., Meyers, C.A., Klein, R.L., King, M.A., Hughes, J.A., Memory-related deficits following selective hippocampal expression of Swedish mutation amyloid precursor protein in the rat. Exp. Neurol. 200 (2006), 371–377.
12. [12] Haass, C., Selkoe, D.J., Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide. Nat. Rev. Mol. Cell. Biol. 8 (2007), 101–112.
13. [13] Kirkitadze, M.D., Bitan, G., Teplow, D.B., Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: the emerging role of oligomeric assemblies. J. Neurosci. Res. 69 (2002), 567–577.
14. [14] Larson, J., Lynch, G., Games, D., Seubert, P., Alterations in synaptic transmission and long-term potentiation in hippocampal slices from young and aged PDAPP mice. Brain Res. 840 (1999), 23–35.
15. [15] Näslund, J., Haroutunian, V., Mohs, R., Davis, K.L., Davies, P., Greengard, P., Buxbaum, J.D., Correlation between elevated levels of amyloid β-peptide in the brain and cognitive decline. JAMA 283 (2000), 1571–1577.
16. [16] Stine, W.B. Jr., Dahlgren, K.N., Krafft, G.A., LaDu, M.J., In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis. J. Biol. Chem. 278 (2003), 11612–11622.
17. [17] Teplow, D.B., On the subject of rigor in the study of amyloid β-protein assembly. Alzheimers Res. Ther., 5, 2013, 39.
18. [18] Jan, A., Adolfsson, O., Allaman, I., Buccarello, A.L., Magistretti, P.J., Pfeifer, A., Muhs, A., Lashuel, H.A., Aβ42 neurotoxicity is mediated by ongoing nucleated polymerization process rather than by discrete Aβ42 species. J. Biol. Chem. 286 (2011), 8585–8596.
19. [19] Bitan, G., Lomakin, A., Teplow, D.B., Amyloid β-protein oligomerization: prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins. J. Biol. Chem. 276 (2001), 35176–35184.
20. [20] Fancy, D.A., Kodadek, T., Chemistry for the analysis of protein-protein interactions: rapid and efficient cross-linking triggered by long wavelength light. Proc. Natl. Acad. Sci. U. S. A. 96 (1999), 6020–6024.
21. [21] Bitan, G., Teplow, D.B., Rapid photochemical cross-linking–a new tool for studies of metastable, amyloidogenic protein assemblies. Acc. Chem. Res. 37 (2004), 357–364.
22. [22] Ono, K., Condron, M.M., Teplow, D.B., Structure-neurotoxicity relationships of amyloid β-protein oligomers. Proc. Natl. Acad. Sci. U. S. A. 106 (2009), 14745–14750.
23. [23] Yang, M., Teplow, D.B., Amyloid β-protein monomer folding: free-energy surfaces reveal alloform-specific differences. J. Mol. Biol. 384 (2008), 450–464.
24. [24] Bernstein, S.L., Dupuis, N.F., Lazo, N.D., Wyttenbach, T., Condron, M.M., Bitan, G., Teplow, D.B., Shea, J.E., Ruotolo, B.T., Robinson, C.V., Bowers, M.T., Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease. Nat. Chem. 1 (2009), 326–331.
25. [25] Ball, K.A., Phillips, A.H., Wemmer, D.E., Head-Gordon, T., Differences in β-strand populations of monomeric Aβ40 and Aβ42. Biophys. J. 104 (2013), 2714–2724.
26. [26] Yan, Y., Wang, C., Aβ42 is more rigid than Aβ40 at the C terminus: implications for Aβ aggregation and toxicity. J. Mol. Biol. 364 (2006), 853–862.
27. [27] Yamin, G., Huynh, T.P., Teplow, D.B., Design and characterization of chemically stabilized Aβ42 oligomers. Biochemistry 54 (2015), 5315–5321.
28. [28] Maji, S.K., Amsden, J.J., Rothschild, K.J., Condron, M.M., Teplow, D.B., Conformational dynamics of amyloid β-protein assembly probed using intrinsic fluorescence. Biochemistry 44 (2005), 13365–13376.
29. [29] Fezoui, Y., Hartley, D.M., Harper, J.D., Khurana, R., Walsh, D.M., Condron, M.M., Selkoe, D.J., Lansbury, P.T. Jr., Fink, A.L., Teplow, D.B., An improved method of preparing the amyloid β-protein for fibrillogenesis and neurotoxicity experiments. Amyloid 7 (2000), 166–178.
30. [30] Cleveland, D.W., Fischer, S.G., Kirschner, M.W., Laemmli, U.K., Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis. J. Biol. Chem. 252 (1977), 1102–1106.
31. [31] Kawooya, J.K., Emmons, T.L., Gonzalez-DeWhitt, P.A., Camp, M.C., D'Andrea, S.C., Electrophoretic mobility of Alzheimer's amyloid-β peptides in urea-sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Anal. Biochem. 323 (2003), 103–113.