Surface-modified magnetite nanoparticles affect lysozyme amyloid fibrillization

The surface of nanoparticles (NPs) is an important factor affecting the process of poly/peptides' amyloid aggregation. We have investigated the in vitro effect of trisodium citrate (TC), gum arabic (GA) and citric acid (CA) surface-modified magnetite nanoparticles (COAT-MNPs) on hen egg-white l...

Full description

Saved in:
Bibliographic Details
Published in:Biochimica et biophysica acta. General subjects Vol. 1865; no. 9; p. 129941
Main Authors: Antosova, A., Gancar, M., Bednarikova, Z., Marek, J., Zahn, D., Dutz, S., Gazova, Z.
Format: Journal Article
Language:English
Published: Elsevier B.V 01-09-2021
Subjects:
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The surface of nanoparticles (NPs) is an important factor affecting the process of poly/peptides' amyloid aggregation. We have investigated the in vitro effect of trisodium citrate (TC), gum arabic (GA) and citric acid (CA) surface-modified magnetite nanoparticles (COAT-MNPs) on hen egg-white lysozyme (HEWL) amyloid fibrillization and mature HEWL fibrils. Dynamic light scattering (DLS) was used to characterize the physico-chemical properties of studied COAT-MNPs and determine the adsorption potential of their surface towards HEWL. The anti-amyloid properties were studied using thioflavin T (ThT) and tryptophan (Trp) intrinsic fluorescence assays, and atomic force microscopy (AFM). The morphology of amyloid aggregates was analyzed using Gwyddion software. The cytotoxicity of COAT-MNPs was determined utilizing Trypan blue (TB) assay. Agents used for surface modification affect the COAT-MNPs physico-chemical properties and modulate their anti-amyloid potential. The results from ThT and intrinsic fluorescence showed that the inhibitory activities result from the more favorable interactions of COAT-MNPs with early pre-amyloid species, presumably reducing nuclei and oligomers formation necessary for amyloid fibrillization. COAT-MNPs also possess destroying potential, which is presumably caused by the interaction with hydrophobic residues of the fibrils, resulting in the interruption of an interface between β-sheets stabilizing the amyloid fibrils. COAT-MNPs were able to inhibit HEWL fibrillization and destroy mature fibrils with different efficacy depending on their properties, TC-MNPs being the most potent nanoparticles. The study reports findings regarding the general impact of nanoparticles' surface modifications on the amyloid aggregation of proteins. [Display omitted] •Surface-modified magnetic nanoparticles (MNPs) affect lysozyme amyloid aggregation.•Surface modification determines the anti-amyloid activity of nanoparticles.•Trisodium citrate magnetic nanoparticles (TC-MNPs) - the most effective inhibitors
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0304-4165
1872-8006
DOI:10.1016/j.bbagen.2021.129941