Effect of plasmonic excitation on mature insulin amyloid fibrils

Interactions between amyloid protein structures and nanomaterials have been extensively studied to develop effective inhibitors of amyloid aggregation. Limited investigations are reported on the impact of nanoparticles on mature fibrils. In this work, gold nanoparticles are used as photothermal agen...

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Published in:Colloids and surfaces, B, Biointerfaces Vol. 228; p. 113434
Main Authors: Cambiotti, Elena, Bednarikova, Zuzana, Gazova, Zuzana, Sassi, Paola, Bystrenova, Eva, Latterini, Loredana
Format: Journal Article
Language:English
Published: Netherlands Elsevier B.V 01-08-2023
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Summary:Interactions between amyloid protein structures and nanomaterials have been extensively studied to develop effective inhibitors of amyloid aggregation. Limited investigations are reported on the impact of nanoparticles on mature fibrils. In this work, gold nanoparticles are used as photothermal agents to alter insulin fibrils. To this end, gold colloids bearing a negatively charged capping shell, with an average diameter of 14 nm and a plasmon resonance maximum at 520 nm are synthesized. The effects on mature insulin fibril morphology and structure upon plasmonic excitation of the nanoparticles-fibril samples have been monitored by spectroscopic and microscopic methods. The obtained data indicate that an effective destruction of the amyloid aggregates occur upon irradiation of the plasmonic nanoparticles, allowing the development of emerging strategies to alter the structure of amyloid fibrils. [Display omitted] •Gold Nanoparticles (AuNPs) and Insulin Fibrils (IF) are prepared.•Electrostatic interactions drive the adsorption of AuNPs on IF.•Plasmonic excitation of AuNPs/IF complex activates the photothermal effect.•Fluorescence assay and microscopies used to monitor IF during plasmonic excitation.•Photothermal effect induces modifications on the morphology and structure of IF.
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ISSN:0927-7765
1873-4367
DOI:10.1016/j.colsurfb.2023.113434