Effect of plasmonic excitation on mature insulin amyloid fibrils

Colloids Surf B Biointerfaces. 2023 Aug:228:113434. doi: 10.1016/j.colsurfb.2023.113434. Epub 2023 Jun 29.

Abstract

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.

Keywords: Amyloid aggregates; Destructuring effects; Gold nanoparticles; Insulin fibrils; Photothermal effect; Surface plasmonic resonance.

MeSH terms

  • Amyloid* / chemistry
  • Amyloidogenic Proteins
  • Gold / chemistry
  • Insulin / chemistry
  • Metal Nanoparticles*

Substances

  • Amyloid
  • Insulin
  • Gold
  • Amyloidogenic Proteins