Gold nanocolloid–protein interactions and their impact on β-sheet amyloid fibril formation

Barros, Heloise Ribeiro de; Kokkinopoulou, Maria; Riegel‐Vidotti, Izabel C.; Landfester, Katharina; Thérien-Aubin, Héloı̈se

doi:10.1039/c7ra11219j

Cited by 12 publications

(4 citation statements)

References 53 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…where the alignment of beta‐lactoglobulin fibrils doped with magnetite nanoparticles was achieved by using an external magnetic field . Research works dealing with the effects of various types of particles (gold, silver) on amyloid fibril (insulin, beta‐lactoglobulin) behaviour have been reported previously. For instance, in Ma et al ., it was observed that the change in concentration of zinc ions has no significant influence on fibril morphology, though it has influenced the level of fibril inhibition.…”

Section: Resultsmentioning

confidence: 99%

Effect of the concentration of protein and nanoparticles on the structure of biohybrid nanocomposites

et al. 2019

View full text Add to dashboard Cite

We present colloidal nanocomposites formed by incorporating magnetite Fe3O4 nanoparticles (MNPs) with lysozyme amyloid fibrils (LAFs). Preparation of two types of solutions, with and without addition of salt, was carried out to elucidate the structure of MNPs‐incorporated fibrillary nanocomposites and to study the effect of the presence of salt on the stability of the nanocomposites. The structural morphology of the LAFs and their interaction with MNPs were analyzed by atomic force microscopy and small‐angle x‐ray scattering measurements. The results indicate that conformational properties of the fibrils are dependent on the concentration of protein, and the precise ratio of the concentration of the protein and MNPs is crucially important for the stability of the fibrillary nanocomposites. Our results confirm that despite the change in fibrillary morphology induced by the varying concentration of the protein, the adsorption of MNPs on the surface of LAF is morphologically independent. Moreover, most importantly, the samples containing salt have excellent stability for up to 1 year of shelf‐life.

show abstract

Section: Resultsmentioning

confidence: 99%

Effect of the concentration of protein and nanoparticles on the structure of biohybrid nanocomposites

et al. 2019

View full text Add to dashboard Cite

show abstract

“…To date, polyphenols, mostly naturally occurring organic molecules, have been identified as blocking factors in amyloidogenesis [3][4][5] . Recently, there has been growing interest in the use of biocompatible inert metal nanoparticles (NPs) [6][7][8] , both as inhibitors of protein aggregation [9][10][11] and folding assistants, analogous to molecular chaperones 12 . Consequently, the elucidation of the underlying molecular mechanisms of NPs-fibrils interaction is a crucial point for the actual therapeutic employment of NPs.…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2021

View full text Add to dashboard Cite

show abstract

“…Some NPs were already shown to induce 11–13 or prevent 14,15 fibrillation of amyloid peptides, depending on their sizes, shapes, hydrophobicity and other parameters. It might be particularly interesting to prepare NPs that can affect the formation, growth, and breaking of amyloid fibrils structures 16 , in analogy to polymer-peptide conjugates that can break amyloid fibrils 17 .…”

Section: Introductionmentioning

confidence: 99%

Computational screening of nanoparticles coupling to Aβ40 peptides and fibrils

Sen

Vuković

2019

Sci Rep

View full text Add to dashboard Cite

Blocking the formation, growth, and breaking of amyloid fibrils by synthetic nanosystems could provide a treatment of neurodegenerative diseases. With this in mind, here atomistic molecular dynamics simulations are used to screen for nanoparticles (NPs), covered with different mixtures of ligands, including positively and negatively charged ligands, Aβ40-cut-peptide, and synthetic inhibitor ligands, in their selective coupling to Aβ40 peptides and their fibrils. The simulations reveal that only Aβ40-cut-peptide-covered NPs have strong and selective coupling to Aβ40 monomers. On the other hand, positive, positive-neutral, Janus, and peptide NPs couple to the beta sheet surfaces of Aβ40 fibrils and only the negative-neutral NPs couple to the fibril tips.

show abstract

Gold nanocolloid–protein interactions and their impact on β-sheet amyloid fibril formation

Abstract: Formation of amyloid protein fibrils is associated with degenerative diseases. Here, the interaction mechanism between globular and fibrillar proteins with AuNPs were investigated in order to potentially control and reverse the fibrillation process.

Cited by 12 publications

References 53 publications

Effect of the concentration of protein and nanoparticles on the structure of biohybrid nanocomposites

Effect of the concentration of protein and nanoparticles on the structure of biohybrid nanocomposites

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

Computational screening of nanoparticles coupling to Aβ40 peptides and fibrils

Contact Info

Product

Resources

About