期刊
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
卷 1865, 期 9, 页码 -出版社
ELSEVIER
DOI: 10.1016/j.bbagen.2021.129941
关键词
Hen egg-white lysozyme; Amyloid aggregation; Magnetite nanoparticles; Trisodium citrate; Gum arabic; Citric acid
资金
- Slovak Research and Developement Agency [APVV-18-0284]
- research agency VEGA [2/0176/21]
- Thuringer Innovationszentrum fur Medizintechnik-L osungen (ThIMEDOP) [FKZ IZN 2018 0002]
- Operational Programme Integrated Infrastructure (OPII) - ERDF [DIAGNAD ITMS2014+ 313011T553]
The surface modifications of nanoparticles have significant impact on the aggregation of proteins, specifically on the amyloid fibrillization process. COAT-MNPs were found to inhibit HEWL fibrillization and destroy mature fibrils, with TC-MNPs demonstrating the highest efficacy among the nanoparticles studied.
Background: 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. Methods: 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. Results: 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 beta-sheets stabilizing the amyloid fibrils. Conclusion: 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. General significance: The study reports findings regarding the general impact of nanoparticles' surface modifications on the amyloid aggregation of proteins.
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