ORCID Profile
0000-0003-0500-3545
Current Organisation
University of California, San Diego
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Publisher: MDPI AG
Date: 24-01-2018
DOI: 10.3390/IJMS19020334
Publisher: Springer Science and Business Media LLC
Date: 23-09-2021
DOI: 10.1038/S42003-021-02624-X
Abstract: The aggregation of alpha-synuclein (α-SYN) follows a cascade of oligomeric, prefibrillar and fibrillar forms, culminating in the formation of Lewy Bodies (LB), the pathological hallmarks of Parkinson’s Disease. Although LB contain over 70 proteins, the potential for interactions along the aggregation pathway of α-SYN is unknown. Here we propose a map of interactions of 65 proteins against different species of α-SYN. We measured binding to monomeric α-SYN using AlphaScreen, a sensitive nano-bead luminescence assay for detection of protein interactions. To access oligomeric species, we used the pathological mutants of α-SYN (A30P, G51D and A53T) which form oligomers with distinct properties. Finally, we generated amyloid fibrils from recombinant α-SYN. Binding to oligomers and fibrils was measured by two-color coincidence detection (TCCD) on a single molecule spectroscopy setup. Overall, we demonstrate that LB components are recruited to specific steps in the aggregation of α-SYN, uncovering future targets to modulate aggregation in synucleinopathies.
Publisher: Elsevier BV
Date: 12-2016
Publisher: Elsevier BV
Date: 03-2023
Publisher: Elsevier BV
Date: 10-2023
Publisher: American Association for the Advancement of Science (AAAS)
Date: 24-12-2021
Abstract: Mutant prion protein particles form axonal aggregates inside endolysosomes via axonal transport and endosomal fusion.
Location: United States of America
Location: Portugal
No related grants have been discovered for Andre Leitao.