Peptide concentration alters intermediate species in amyloid β fibrillation kinetics

Biochemical and Biophysical Research Communications

Volumn 433, Issue 3, 2013, Pages 276-280

  Garvey, M ^a,b   Morgado, I ^a  

^a MAX PLANCK RESEARCH UNIT FOR ENZYMOLOGY OF PROTEIN FOLDING   (Germany)

^b RWTH AACHEN UNIVERSITY   (Germany)

Author keywords

Aggregation; Amyloid ; Concentration; Nucleation; Sodium phosphate

Indexed keywords

AMYLOID BETA PROTEIN; PEPTIDE; THIOFLAVINE;

ARTICLE; CONCENTRATION (PARAMETERS); FLUORESCENCE MICROSCOPY; IN VITRO STUDY; KINETICS; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN INTERACTION; TRANSMISSION ELECTRON MICROSCOPY;

AMYLOID BETA-PEPTIDES; FLUORESCENCE; HUMANS; KINETICS; MICROSCOPY, ELECTRON, TRANSMISSION; PEPTIDE FRAGMENTS; PEPTIDES; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SPECTROMETRY, FLUORESCENCE; THIAZOLES;

EID: 84876321326     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2013.02.073     Document Type: Article

References (14)

1. Wetzel R. Kinetics and thermodynamics of amyloid fibril assembly. Acc. Chem. Res. 2006, 39:671-679.
2. Harper J.D., Lansbury P.T. Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu. Rev. Biochem. 1997, 66:385-407.
3. Knowles T.P., Waudby C.A., Devlin G.L., Cohen S.I., Aguzzi A., Vendruscolo M., Terentjev E.M., Welland M.E., Dobson C.M. An analytical solution to the kinetics of breakable filament assembly. Science 2009, 326:1533-1537.
4. Walsh D.M., Lomakin A., Benedek G.B., Condron M.M., Teplow D.B. Amyloid beta-protein fibrillogenesis. Detection of a protofibrillar intermediate. J. Biol. Chem. 1997, 272:22364-22372.
5. Goldsbury C.S., Wirtz S., Muller S.A., Sunderji S., Wicki P., Aebi U., Frey P. Studies on the in vitro assembly of a beta 1-40: implications for the search for a beta fibril formation inhibitors. J. Struct. Biol. 2000, 130:217-231.
6. Garvey M., Tepper K., Haupt C., Knupfer U., Klement K., Meinhardt J., Horn U., Balbach J., Fandrich M. Phosphate and HEPES buffers potently affect the fibrillation and oligomerization mechanism of Alzheimer's Aβ peptide. Biochem. Biophys. Res. Commun. 2011, 409:385-388.
7. Hortschansky P., Schroeckh V., Christopeit T., Zandomeneghi G., Fandrich M. The aggregation kinetics of Alzheimer's beta-amyloid peptide is controlled by stochastic nucleation. Protein Sci. 2005, 14:1753-1759.
8. Chiti F., Taddei N., Baroni F., Capanni C., Stefani M., Ramponi G., Dobson C.M. Kinetic partitioning of protein folding and aggregation. Nat. Struct. Biol. 2002, 9:137-143.
9. Xue W.-F., Homans S.W., Radford S.E. Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly. Proc. Natl. Acad. Sci. USA 2008, 105:8926-8931.
10. Huang T.H.J., Yang D.-S., Fraser P.E., Chakrabartty A. Alternate aggregation pathways of the Alzheimer beta-amyloid peptide: an in vitro model of preamyloid. J. Biol. Chem. 2000, 275:36436-36440.
11. Lin M.-S., Chen L.-Y., Tsai H.-T., Wang S.S.S., Chang Y., Higuchi A., Chen W.-Y. Investigation of the mechanism of beta-amyloid fibril formation by kinetic and thermodynamic analyses. Langmuir 2008, 24:5802-5808.
12. Padrick S.B., Miranker A.D. Islet amyloid: phase partitioning and secondary nucleation are central to the mechanism of fibrillogenesis. Biochemistry 2002, 41:4694-4703.
13. Meinhardt J., Sachse C., Hortschansky P., Grigorieff N., Fändrich M. A beta(1-40) fibril polymorphism implies diverse interaction patterns in amyloid fibrils. J. Mol. Biol. 2009, 386:869-877.
14. Pedersen J.S., Dikov D., Flink J.L., Hjuler H.A., Christiansen G., Otzen D.E. The changing face of glucagon fibrillation: structural polymorphism and conformational imprinting. J. Mol. Biol. 2006, 355:501-523.