Fluorescence of Aggregated Aromatic Peptides for Studying the Kinetics of Aggregation and Hardening of Amyloid‐like Structures

Abstract

AbstractThe capability of amyloid‐like peptide fibers to emit intrinsic‐fluorescence enables the study of their formation, stability and hardening through time‐resolved fluorescence analysis, without the need for additional intercalating dyes. This approach allows the monitoring of amyloid‐like peptides aggregation kinetics using minimal sample volumes, and the simultaneous testing of numerous experimental conditions and analytes, offering rapid and reproducible results. The analytical procedure applied to the aromatic hexapeptide F6, alone or derivatized with PEG (polyethylene glycol) moiety of different lengths, suggests that aggregation into large anisotropic structures negatively correlates with initial monomer concentration and relies on the presence of charged N‐ and C‐termini. PEGylation reduces the extent of aggregates hardening, possibly by retaining water, and overall impacts the final structural properties of the aggregates.