Details

Autor(en) / Beteiligte

• Song, Linyan
• Wang, Junjie
• Duan, Wei

Titel

Denatured BSA-mediated co-assembly with iron oxide nanoparticles and their effect on protein fibrillation

Ist Teil von

• Chemical physics letters, 2023-11, Vol.830, p.140790, Article 140790

Ort / Verlag

Elsevier B.V

Erscheinungsjahr

2023

Quelle

Access via ScienceDirect (Elsevier)

Beschreibungen/Notizen

• In vitro inhibition of Lyz fibrillation by bare IONPs and protein crown coated IONPs. [Display omitted] •Denatured BSA led to co-assemble with IONPs into a size-limited core–shell structure.•The mechanism of denatured BSA and IONPs co-assemble was confirmed.•BSA and denatured BSA capped IONPs weakened the anti Lyz fibrillation effects of bare IONPs.•Bare /BSA and denatured BSA capped IONPs had different interactions with Lyz during fibrillation. Understanding the interaction between nanoparticles (NPs) and proteins provides a preliminary foundation for the further biomedical application of NPs. Herein, we disclosed that, unlike the natural bovine serum albumin (BSA) that interacts with iron oxide NPs (IONPs) to form a monolayer protein crown, the denatured BSA could co-assemble with IONPs to form stable protein coronal aggregates. Moreover, the effects of protein crown encapsulated IONPs on the anti-fibrotic ability was investigated. It was found that formation of protein crown on IONPs resulted in a weakened anti-fibrillation effect. Nevertheless, such adverse effect could be minimized by denatured BSA induced stable protein coronal aggregates.