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 |
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Main Authors: | , , , , , |
Format: | Journal Article |
Language: | English |
Published: |
Netherlands
Elsevier B.V
01-08-2023
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Subjects: | |
Online Access: | Get full text |
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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.
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•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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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0927-7765 1873-4367 |
DOI: | 10.1016/j.colsurfb.2023.113434 |