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• W2900696587 abstract "Inhibiting protein aggregation under intra-/extracellular space and clearing protein aggregates from the brain are two critical issues for the treatment of various neurodegenerative diseases. Although a variety of anti-amyloidogenic chemicals/biochemicals have been identified for inhibiting such protein aggregation, clearing protein aggregates is a challenging issue. Here we report a designed biopolymer micelle of 15-30 nm hydrodynamic size that can clear protein aggregates from cells via an up-regulated autophagy process. The polymer has a polyaspartic acid backbone and is functionalized with fatty amine, arginine, and primary amine for inducing self-assembly, enhancing cell uptake, and up-regulating autophagy processes, respectively. The polymer micelle (PM) enters into the cell via lipid raft endocytosis, is transported to the perinuclear region where the protein oligomer/aggregate predominantly localizes, clears aggregated protein from the cell, and enhances the cell's survival against toxic protein aggregates. The designed PM may be used as a drug delivery carrier for anti-amyloidogenic drugs for enhanced efficacy in the treatment of neurodegenerative diseases." @default.
• W2900696587 created "2018-11-29" @default.
• W2900696587 creator A5008830216 @default.
• W2900696587 creator A5023276001 @default.
• W2900696587 creator A5070309679 @default.
• W2900696587 date "2018-11-25" @default.
• W2900696587 modified "2023-09-24" @default.
• W2900696587 title "Designed Polymer Micelle for Clearing Amyloid Protein Aggregates via Up-Regulated Autophagy" @default.
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• W2900696587 doi "https://doi.org/10.1021/acsbiomaterials.8b01196" @default.
• W2900696587 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/33405873" @default.
• W2900696587 hasPublicationYear "2018" @default.
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