Alpha-synuclein — an abundant brain protein
whose function has yet to be clearly defined
— undergoes aggregation and misfolding in
certain forms of PD, as well as dementia with
Lewy bodies (DLB) and AD. The mechanism
of aggregation is uncharacterized mainly
because techniques used to study such
aggregates — as well as their interactions
with other compounds — have many flaws.
Most biophysical methods can't study
protein aggregates — they require
large amounts of sample input and are
highly sensitive to buffer conditions or
background noise. MST, on the other
hand, requires less amount of sample, is
compatible with many buffers, and can be
Measure the physicochemical
properties of alpha-synuclein
aggregates associated with
Parkinson's Disease
1
Molecular
interactions
studied
Target: alpha-synuclein
(monomeric, oligomeric,
fibrillar forms)
Ligands: Nb Syn2
antibody, EGCG
Methods
MST using Monolith
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applied for high throughput screening of
therapeutic drugs or diagnostic targets.
In this study, researchers established
MST to quantify binding interactions
of supramolecular alpha-synuclein
aggregates with compounds of interest.
The authors determined the electrophoretic
mobility of each form of alpha-synuclein, as
well as binding affinities to several types of
ligands. In addition, these data established
the possibility of characterizing and screening
for ligands and binding partners of protein
aggregates, which was previously considered
not possible for amyloid fibrils.
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