Fibrillar aggregates of alpha-synuclein and tau are pathological hallmarks of PD and
AD, respectively. Imaging techniques like positron emission tomography (PET) can
detect fibrils and provide a way to diagnose these diseases. However, there's a large
gap in our understanding of the binding interactions between these fibrillar protein
aggregates and the radioligands used in PET.
Radioligand binding assays and fluorescent competition assays have historically
been used to study interactions between small molecules and the fibrillar forms
of alpha-synuclein and tau. This study was designed as a proof of principle to
assess the utility of MST to detect and characterize the interactions of small
molecules with alpha-synuclein and tau fibrils.
Using MST, binding affinities were determined for fibrillar alpha-synuclein and
tau with compounds previously reported using radioligand binding assays and
fluorescent competition assays. Advantages of using MST over these methods include
the low amounts of sample required for the experiments and overall high sensitivity.
Characterize interactions
between small molecules
and fibrils to develop early
diagnostic tools
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Molecular
interactions
studied
Targets: alpha-synuclein,
tau fibrils
Ligands: SIL26, SU4312,
ThT, thiazine red, T807
Method
MST using Monolith
Learn more
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