AI Article Synopsis
- Amyloid-like peptide fibers can emit intrinsic fluorescence, allowing researchers to study their formation and stability through time-resolved fluorescence analysis without needing extra dyes.
- This method enables the examination of peptide aggregation kinetics with small sample volumes and the ability to test multiple experimental conditions quickly and reliably.
- The research on the hexapeptide F6 reveals that larger aggregates form less when there's a higher initial concentration of monomers and that PEGylation helps retain water, impacting the structural properties of the aggregates.
Article Abstract
The 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.
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| http://dx.doi.org/10.1002/chem.202401998 | DOI Listing |
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