Probing the effect of the molecular interface of gold nanoparticles on the disassembly of insulin amyloid fibrils

C Taverna; C Fasolato; F Brasili; F Ripanti; C Rizza; A De Marcellis; P Postorino; S Sennato; A Nucara; A Capocefalo

doi:10.1016/j.ijbiomac.2025.141735

Probing the effect of the molecular interface of gold nanoparticles on the disassembly of insulin amyloid fibrils

Int J Biol Macromol. 2025 May;306(Pt 3):141735. doi: 10.1016/j.ijbiomac.2025.141735. Epub 2025 Mar 3.

Authors

C Taverna¹, C Fasolato², F Brasili², F Ripanti³, C Rizza⁴, A De Marcellis⁵, P Postorino⁶, S Sennato², A Nucara⁷, A Capocefalo⁸

Affiliations

¹ Physics Department, Sapienza University of Rome, P.le Aldo Moro, 5, Rome 00185, Italy; Synchrotron SOLEIL, L'Orme des Merisiers, Saint-Aubin 91192, France.
² Institute for Complex Systems, National Research Council, P.le Aldo Moro, 5, Rome 00185, Italy.
³ Department of Life and Environmental Sciences, Marche Polytechnic University, Via Brecce Bianche, Ancona 60131, Italy.
⁴ Department of Physical and Chemical Sciences, University of L'Aquila, via Vetoio, L'Aquila 67100, Italy.
⁵ Department of Information Engineering, Computer Science and Mathematics, University of L'Aquila, via Vetoio, L'Aquila 67100, Italy.
⁶ Physics Department, Sapienza University of Rome, P.le Aldo Moro, 5, Rome 00185, Italy.
⁷ Physics Department, Sapienza University of Rome, P.le Aldo Moro, 5, Rome 00185, Italy. Electronic address: alessandro.nucara@uniroma1.it.
⁸ Department of Physical and Chemical Sciences, University of L'Aquila, via Vetoio, L'Aquila 67100, Italy. Electronic address: angela.capocefalo@univaq.it.

PMID: 40043982
DOI: 10.1016/j.ijbiomac.2025.141735

Abstract

Aberrant protein aggregation into amyloid fibrils underlies the onset of several degenerative pathologies, requiring increasing efforts to identify ever newer approaches to prevent their formation and to disassemble toxic amyloid structures. In this context, gold nanoparticles (AuNPs) show great promise, thanks to their ability to chemically interact with proteins while simultaneously serving as local spectroscopic probes due to their peculiar optical properties. Here, we investigate the role of the surface chemistry of AuNPs in the disassembly of insulin amyloid fibrils. By taking advantage of the remarkable sensitivity and spatial resolution of surface enhanced Raman spectroscopy, we elucidate the molecular mechanisms driving fibril-AuNP interaction at the nanoscale, identifying the amino acids directly involved. The obtained results will serve as a benchmark for developing novel diagnostic and therapeutic strategies employing AuNPs for the treatment of amyloid-related diseases.

Keywords: Amyloid fibrils; Circular dichroism; Gold nanoparticles; Insulin; Surface enhanced Raman spectroscopy.

MeSH terms

Amyloid* / chemistry
Gold* / chemistry
Insulin* / chemistry
Metal Nanoparticles* / chemistry
Protein Aggregates
Spectrum Analysis, Raman

Substances

Gold
Insulin
Amyloid
Protein Aggregates