Ludwig-Maximilians-Universität, Chair of Metabolic Biochemistry

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Single particle detection and characterization of synuclein co-aggregation

Biochem Biophys Res Commun 333(4): 1202-10

Authors/Editors: Giese A
Bader B
Bieschke J
Schaffar G
Odoy S
Kahle PJ
Haass C
Kretzschmar H
Publication Date: 2005
Type of Publication: Journal Article
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.

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