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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Giese, A. et al.

Giese, Bader, Bieschke, Schaffar, Odoy, Kahle, Haass, Kretzschmar,

Single particle detection and characterization of synuclein co-aggregation.

Protein aggregation is the key event in a number of human diseases such as Alzheimer's and Parkinson's disease. We present a general method to quantify and characterize protein aggregates by dual-colour scanning for intensely fluorescent targets (SIFT). In addition to high sensitivity, this approach offers a unique opportunity to study co-aggregation processes. As the ratio of two fluorescently labelled components can be analysed for each aggregate separately in a homogeneous assay, the molecular composition of aggregates can be studied even in samples containing a mixture of different types of aggregates. Using this method, we could show that wild-type alpha-synuclein forms co-aggregates with a mutant variant found in familial Parkinson's disease. Moreover, we found a striking increase in aggregate formation at non-equimolar mixing ratios, which may have important therapeutic implications, as lowering the relative amount of aberrant protein may cause an increase of protein aggregation leading to adverse effects.[1]

References

Single particle detection and characterization of synuclein co-aggregation. Giese, A., Bader, B., Bieschke, J., Schaffar, G., Odoy, S., Kahle, P.J., Haass, C., Kretzschmar, H. Biochem. Biophys. Res. Commun. (2005) [Pubmed]

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