Cavity Lasing\nof Thioflavin T in the Condensed Phase\nfor Discrimination between Surface Interaction and β‑Sheet\nGroove Binding in Alzheimer-Linked Peptides

This study investigates the lasing effects in a Fabry–Perot\ncavity to discern the binding interactions of thioflavin T (ThT) with\nvarious peptides associated with Alzheimer’s disease, including\nAβ(1–42), KLVFFA, and diphenylalanine (FF) in the condensed\nphase. Utilizing kinetic lasing measurements, the research explores\nThT emission enhancements due to specific groove binding in β-sheet\nstructures and highlights additional contributions from weak surface\ninteractions and solvent–solute interactions. Lasing spectroscopy\nreveals a lack of transition of the FF system from its native state\nto an amyloid-like structure, challenging traditional ThT assay interpretations.\nThese findings show the potential of lasing spectroscopy in elucidating\nthe molecular basis of amyloid fibril formation and the development\nof diagnostic tools for amyloidogenic diseases.

Publication Details

Journal
Figshare
Published
2024-09-12
DOI
https://doi.org/10.1021/acs.jpclett.4c01709.s001
Primary Topic
Spectroscopy and Quantum Chemical Studies
Type
article
Field-Weighted Citation Impact
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article

Cavity Lasing\nof Thioflavin T in the Condensed Phase\nfor Discrimination between Surface Interaction and β‑Sheet\nGroove Binding in Alzheimer-Linked Peptides

Figshare
Spectroscopy and Quantum Chemical Studies
article

Cavity Lasing\nof Thioflavin T in the Condensed Phase\nfor Discrimination between Surface Interaction and β‑Sheet\nGroove Binding in Alzheimer-Linked Peptides

article en

Abstract

This study investigates the lasing effects in a Fabry–Perot\ncavity to discern the binding interactions of thioflavin T (ThT) with\nvarious peptides associated with Alzheimer’s disease, including\nAβ(1–42), KLVFFA, and diphenylalanine (FF) in the condensed\nphase. Utilizing kinetic lasing measurements, the research explores\nThT emission enhancements due to specific groove binding in β-sheet\nstructures and highlights additional contributions from weak surface\ninteractions and solvent–solute interactions. Lasing spectroscopy\nreveals a lack of transition of the FF system from its native state\nto an amyloid-like structure, challenging traditional ThT assay interpretations.\nThese findings show the potential of lasing spectroscopy in elucidating\nthe molecular basis of amyloid fibril formation and the development\nof diagnostic tools for amyloidogenic diseases.

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Spectroscopy and Quantum Chemical Studies
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