Abstract
Misfolded proteins produce fibrillar aggregates, which contain β-sheet higher order structures. The oligomers, protofibrils, and fibrils generated during protein aggregation process are cytotoxic and can cause various neurodegenerative diseases. Recently the photo-active materials, the photosensitizers, have attracted increased attention in the study and treatment of amyloid-related diseases. Here, we studied the photodynamic effect of the amyloid-specific fluorescence dye Thioflavin T on the formation of self-assembled peptide hydrogel. It was demonstrated that the gelation process under irradiation inhibits significantly, at that the structural and mechanical properties of mature fibrils change notably suggesting that ThT could be regarded as a theranostic probe. The developed peptide model allows for quantification of the photodynamic agent’s efficiency in preventing aggregation, thus paving the way for a high-throughput test system for screening of light-responsive theranostic agents.
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