4.8 Article

Unveiling the interaction of protein fibrils with gold nanoparticles by plasmon enhanced nano-spectroscopy

Journal

NANOSCALE
Volume 13, Issue 34, Pages 14469-14479

Publisher

ROYAL SOC CHEMISTRY
DOI: 10.1039/d1nr03190b

Keywords

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Funding

  1. Sapienza University [AR11816436CE4810]
  2. Joint Research Projects for the mobility of PhD students
  3. German Science Foundation DFG [CRC/SFB 1375 NOA - C2]
  4. DFG [448666227]
  5. Leibniz Science Campus InfectoOptics via Project HoTAiM 2.0

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This study investigates the role of gold nanoparticles in degrading amyloid fibrils and reveals molecular mechanisms using high-resolution Raman spectroscopy, providing important insights for understanding amyloid fibrils and potential implications for developing strategies to prevent and treat amyloid-related diseases.
The development of various degenerative diseases is suggested to be triggered by the uncontrolled organisation and aggregation of proteins into amyloid fibrils. For this reason, there are ongoing efforts to develop novel agents and approaches, including metal nanoparticle-based colloids, that dissolve amyloid structures and prevent pathogenic protein aggregation. In this contribution, the role of gold nanoparticles (AuNPs) in degrading amyloid fibrils of the model protein lysozyme is investigated. The amino acid composition of fibril surfaces before and after the incubation with AuNPs is determined at the single fibril level by exploiting the high spatial resolution and sensitivity provided by tip-enhanced and surface-enhanced Raman spectroscopies. This combined spectroscopic approach allows to reveal the molecular mechanisms driving the interaction between fibrils and AuNPs. Our results provide an important input for the understanding of amyloid fibrils and could have a potential translational impact on the development of strategies for the prevention and treatment of amyloid-related diseases.

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