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...
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Published in: | Biochimica et biophysica acta. General subjects Vol. 1865; no. 9; p. 129941 |
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Main Authors: | , , , , , , |
Format: | Journal Article |
Language: | English |
Published: |
Elsevier B.V
01-09-2021
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Subjects: | |
Online Access: | Get full text |
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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.
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•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 |
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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 |