Examining the effects of dextran-based polymer-coated nanoparticles on amyloid fibrillogenesis of human insulin

Colloids and Surfaces. B, Biointerfaces
Ning-Hui LuSteven S-S Wang

Abstract

More than thirty human proteins and/or peptides can aggregate to form amyloid deposits that are linked to several amyloid diseases including clinical syndrome injection-localized amyloidosis, which is correlated with the aggregation of the 51-residue polypeptide insulin. While no cure is currently available toward tackling amyloid diseases, prevention or suppression of amyloid fibrillization is considered as the primary therapeutic strategy. Nanomaterials have been demonstrated to possess great potential in the fields of biomedical diagnosis and drug delivery, they are also able to affect the amyloid aggregation of proteins. This work explores the effects of three different magnetic nanoparticles coated with dextran-based polymers on the in vitro amyloid fibrillogenesis of human insulin. Surface modification of nanoparticles with dextran-based polymers was used to improve the biocompatibility of maghemite nanoparticles. We demonstrated that insulin fibrillization may be mitigated by the studied nanoparticles in a concentration-dependent fashion as verified by ThT binding assay and transmission electron microscopy. The extent of inhibitory activity against human insulin fibril formation was found to be associated with the physico...Continue Reading

Citations

May 14, 2020·Scientific Reports·Brahmaiah MeesaragandlaMihaela Delcea
Sep 30, 2020·Chemical Communications : Chem Comm·Mohsen AkbarianVladimir N Uversky
Mar 8, 2019·Biointerphases·Zahra KhosraviAmir M Farnoud
Mar 9, 2021·Neurochemistry International·Mukta AgrawalAmit Alexander
Sep 23, 2020·International Journal of Biological Macromolecules·Chien-Yu LinSteven S-S Wang
Feb 19, 2020·International Journal of Biological Macromolecules·Anang Kumar SinghAnushree Roy
Jul 13, 2019·ACS Chemical Neuroscience·Kleoniki GiannousiCatherine Dendrinou-Samara

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