These authors equally contributed to this work.
A synthetic amino acid substitution of Tyr10 in Aβ peptide sequence yields a dominant negative variant in amyloidogenesis
Article first published online: 9 APR 2012
© 2012 The Authors. Aging Cell © 2012 Blackwell Publishing Ltd/Anatomical Society of Great Britain and Ireland
Volume 11, Issue 3, pages 530–541, June 2012
How to Cite
Mazargui, H., Lévêque, C., Bartnik, D., Fantini, J., Gouget, T., Melone, M. A. B., Funke, S. A., Willbold, D. and Perrone, L. (2012), A synthetic amino acid substitution of Tyr10 in Aβ peptide sequence yields a dominant negative variant in amyloidogenesis. Aging Cell, 11: 530–541. doi: 10.1111/j.1474-9726.2012.00814.x
- Issue published online: 11 MAY 2012
- Article first published online: 9 APR 2012
- Accepted manuscript online: 3 MAR 2012 01:46PM EST
- Accepted for publication 27 February 2012
Fig. S1 Analysis of TRITC-wt Aβ (1 μM) binding to SHSY5Y cells both in the presence and absence of increasing concentration unlabelled variant Aβ.
Fig. S2. Analysis of variant (50 μM) and wt Aβ (50 μM) aggregation kinetics in vitro.
Fig. S3 Particle size analysis of wt Aβ, variant Aβ and wt Aβ/variant Aβ mixtures analyzed by dynamic light scattering.
Fig. S4 Variant Aβ does not aggregate in cellulo.
Fig. S5 The dominant negative effect of variant Aβ is specific.
Fig. S6 Variant Aβ shows increased binding to GM1.
Fig. S7 Variant Aβ displays an evident diminished aggregation capability in the presence of synaptosmes.
Fig. S8 Variant Aβ displays an evident diminished aggregation capability in the presence of synaptosmes.
Data S1 Materials and methods.
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