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Modulation of α-Synuclein Aggregation In Vitro by a DNA Aptamer
Claire H Tran1, Ranajay Saha2, Celia Blanco2
1Program in Biomolecular Sciences and Engineering, Department of Chemistry and Biochemistry, University of California, Santa Barbara, California 93106, United States.
Biochemistry
|August 22, 2022
Summary
Nucleic acid aptamers can inhibit protein aggregation. This study shows an aptamer stabilizing off-pathway aggregates, offering a novel mechanism for modulating protein aggregation in diseases like synucleinopathies.
Area of Science:
- Biochemistry
- Molecular Biology
- Biotechnology
Background:
- Protein aggregation is implicated in human diseases and impacts biotechnology.
- Modulating protein aggregation is crucial for therapeutic and production applications.
- Nucleic acid aptamers are potential agents for controlling protein aggregation.
Purpose of the Study:
- To investigate the mechanism by which aptamers modulate alpha-synuclein aggregation.
- To characterize the effect of the T-SO508 aptamer on alpha-synuclein aggregation in vitro.
Main Methods:
- In vitro aggregation kinetics monitored by thioflavin T.
- Characterization of intermediate structures using atomic force microscopy, transmission electron microscopy, and analytical ultracentrifugation.
Main Results:
- The T-SO508 aptamer extended the lag phase of alpha-synuclein aggregation.
- T-SO508 stabilized small, non-fibrillar alpha-synuclein aggregate complexes.
- These aptamer-induced complexes were found to be off-pathway for fibril formation.
Conclusions:
- Aptamers can modulate protein aggregation by stabilizing off-pathway intermediates.
- This mechanism provides insight into aptamer-based therapeutic strategies for protein aggregation disorders.
- The findings highlight a potential role for aptamers in managing synucleinopathies.
