Solid-state optical properties of self-assembling amyloid-like peptides with different charged states at the terminal ends

Autor: Chiara Schiattarella, Luigi Vitagliano, Giancarlo Morelli, Raffaele Velotta, Enrico Gallo, Antonella Accardo, Carlo Diaferia, Bartolomeo Della Ventura
Přispěvatelé: Schiattarella, C., Diaferia, C., Gallo, E., Della Ventura, B., Morelli, G., Vitagliano, L., Velotta, R., Accardo, A.
Rok vydání: 2022
Předmět:
Zdroj: Scientific Reports
Scientific Reports, Vol 12, Iss 1, Pp 1-10 (2022)
ISSN: 2045-2322
DOI: 10.1038/s41598-021-04394-2
Popis: The self-assembling of small peptides not only leads to the formation of intriguing nanoarchitectures, but also generates materials with unexpected functional properties. Oligopeptides can form amyloid-like cross-β assemblies that are able to emit intrinsic photoluminescence (PL), over the whole near-UV/visible range, whose origin is still largely debated. As proton transfer between the peptide chain termini within the assembly is one of the invoked interpretations of this phenomenon, we here evaluated the solid state PL properties of a series of self-assembled hexaphenalanine peptides characterized by a different terminal charge state. Overall, our data indicate that the charge state of these peptides has a marginal role in the PL emission as all systems exhibit very similar multicolour PL associated with a violation of the Kasha’s rule. On the other hand, charged/uncharged ends occasionally produce differences in the quantum yields. The generality of these observations has been proven by extending these analyses to the Aβ16−21 peptide. Collectively, the present findings provide useful information for deciphering the code that links the spectroscopic properties of these assemblies to their structural/electronic features.
Databáze: OpenAIRE
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