Abstract
Alzheimer's disease is characterized by the presence of senile plaques composed of β-amyloid peptide (Aβ) aggregates with toxic effects that are still not fully understood. Recently, it was discovered that Aβ(1–42) fibrils possess catalytic activity on acetylcholine hydrolysis. Catalytic amyloids are an emerging and exciting field of research. In this study, we examined the catalytic activity of the fibrils formed by Aβ(1–40), the most abundant Aβ variant, on acetylcholine hydrolysis. Our findings reveal that Aβ(1–40) fibrils exhibit moderate enzymatic activity, indicating that natural peptide aggregates could serve as biocatalysts and provide new insights into the potential role of Aβ in neurological disorders.
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Funding
This work was financially supported by the Argentinian National Scientific and Technical Research Council (CONICET) of the Ministry of Science, Technology and Innovation under grants PICT-2017-0035, PIP 2017-2019 GI. 112 201701 00462 CO.
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IS and AS: Conceptualization; IS and RS: Methodology; investigation and result analysis: IS (Synthesis and assays), RS (ThT assay); IS: Writing—original draft preparation; IS, RS and AS: Writing—review and editing; AS: Funding acquisition; AS: Supervision.
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Sanchis, I., Spinelli, R. & Siano, A. Acetylcholine hydrolytic activity of fibrillated β-amyloid (1–40) peptide. Amino Acids 55, 1991–1997 (2023). https://doi.org/10.1007/s00726-023-03349-3
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DOI: https://doi.org/10.1007/s00726-023-03349-3