Destroying activity of glycine coated magnetic nanoparticles on lysozyme, α-lactalbumin, insulin and α-crystallin amyloid fibrils

•Protein amyloid aggregation – Hallmark of incurable amyloidosis.•Magnetic nanoparticles – Able to affect amyloid fibrils.•Glycine coated MNPs – Optimal ratio Gly/Fe3O4 is equal to 5/1.•Gly-MNPs interfere with protein amyloid fibrils differently.•Lysozyme, insulin and α-lactalbumin amyloid fibrils a...

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Bibliographic Details
Published in:Journal of magnetism and magnetic materials 2019-02, Vol.471, p.169-176
Main Authors: Antosova, Andrea, Bednarikova, Zuzana, Koneracka, Martina, Antal, Iryna, Zavisova, Vlasta, Kubovcikova, Martina, Wu, Josephine W., S.-S. Wang, Steven, Gazova, Zuzana
Format: Article
Language:English
Subjects:
Amyloid fibrils
Crystal structure
Crystallinity
Dependence
Diabetes mellitus
Enzymes
Glycine
Insulin
Iron oxides
Lysozyme
Magnetic fields
Magnetic nanoparticles
Magnetic properties
Nanoparticles
Proteins
Weight
α-Crystallin
α-Lactalbumin
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Summary:•Protein amyloid aggregation – Hallmark of incurable amyloidosis.•Magnetic nanoparticles – Able to affect amyloid fibrils.•Glycine coated MNPs – Optimal ratio Gly/Fe3O4 is equal to 5/1.•Gly-MNPs interfere with protein amyloid fibrils differently.•Lysozyme, insulin and α-lactalbumin amyloid fibrils are destroyed by Gly-MNPs.•Glycine coated nanoparticles are not able to destroy α-crystallin amyloid fibrils.•Gly-MNPs are promising candidate for treatment of amyloid-related diseases. A great variety of human protein deposition and protein aggregation diseases (Alzheimer’s disease, diabetes mellitus, cataract, systemic amyloidosis and other) have been associated with the accumulation of amyloid fibrils in different tissues. Therefore, development of the agents able to reduce amyloid deposits represents an attractive strategy for their treatment. We have investigated ability of glycine coated magnetic nanoparticles (Gly-MNPs) to destroy protein amyloid fibrils. The properties of Gly-MNPs were characterized with the aim to identify the optimized conditions for the glycine adsorption on surface of MNPs. It was found that Gly-MNPs have superparamagnetic behavior and their size, isoelectric point and stability depend on the amount of the glycine in the samples. The obtained results suggest that optimal weight ratio (w/w) for the modification of MNPs by glycine (Gly/Fe3O4) is equal to 5/1. The selected Gly5-MNPs1 were used for the study of their effect on amyloid fibrils of four globular proteins, namely lysozyme, bovine α-lactalbumin, insulin and α-crystallin. It was found that Gly5-MNPs1 destroy lysozyme, α-lactalbumin and insulin amyloid fibrils in concentration dependence manner. However, Gly5-MNPs1 were not able significantly destroy bovine α-crystallin amyloid fibrils. We assume that obtained results represent important contribution for rational design of potential therapeutics of amyloid diseases based on nanoparticles.
ISSN:0304-8853
1873-4766
DOI:10.1016/j.jmmm.2018.09.096