Lipid-polymer hybrid-vesicles interrupt nucleation of amyloid fibrillation.

ABSTRACT: Solubility and aggregation of proteins are crucial factors for their functional and further biological roles. Aggregation of proteins in vivo, such as the amyloid beta (Aβ_1-40) peptide into fibrils, is significantly modulated by membrane lipids, abundantly present in cells. We developed a model membrane system, composed of lipid hybrid-vesicles bearing embedded hydrophilic polymers to in vitro study the aggregation of the Aβ_1-40 peptide. Focus is to understand and inhibit the primordial, nucleation stages of their fibrillation by added hybrid-vesicles, composed of a natural lipid and amphiphilic polymers. These designed hybrid-vesicles are based on 1-palmitoyl-2-oleoyl-glycero-3-phosphocholine (POPC), displaying embedded hydrophilic (EO) _m

SUBMITTER: Sen N 

PROVIDER: S-EPMC11575630 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature