Oct 2026· Enhanced Spectroscopies and Nanoimaging 2026· 0 citations
Abstract
Tau protein aggregation is a key hallmark of Alzheimer’s disease, making its structural characterization essential for understanding pathological mechanisms and guiding therapeutic strategies. Using tip enhanced Raman spectroscopy (TERS), nanoscale chemical information can be obtained from individual tau aggregates at successive stages of fibril maturation. TERS enabled detection of local secondary structure transitions and clear spectral differentiation between full length tau and the truncated K18 fragment in early aggregation phases. Multivariate data analysis identified vibrational markers of progressive structural ordering, while hyperspectral TERS imaging revealed intrafibrillar heterogeneity resulting from secondary nucleation. Residue specific contributions were also observed, with histidine active at early stages and phenylalanine/tyrosine linked to β sheet stabilization. Nanoscale effects of curcumin as an aggregation inhibitor will also be discussed.
Acknowledgments: This research was funded by National Science Centre, Poland, under the SONATA 17 project (Reg. No. UMO-2021/43/D/ST4/02655).
Tau protein aggregation is one of the key pathological processes driving the global burden of dementia, with Alzheimer's disease being its leading cause. Research on the aggregation pathways and fibrillar structures could provide key insights into the pathogenesis and potential therapeutic approaches for dementia‐relat...
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P. Greco, A. Lazar, F. Lugli et al.· Journal of Colloid and Inter...· 0 citations
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