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Debnath, K and Jana, NR and Jana, Nikhil R (2018) Designed Polymer Micelle for Clearing Amyloid Protein Aggregates via Up-Regulated Autophagy. ACS Biomaterials Science & Engineering, 5 (1). pp. 390-401.

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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.

Item Type: Article
Subjects: Neurodegenerative Disorders
Neuro-Oncological Disorders
Neurocognitive Processes
Neuronal Development and Regeneration
Informatics and Imaging
Genetics and Molecular Biology
Depositing User: Dr. D.D. Lal
Date Deposited: 06 Dec 2019 06:10
Last Modified: 19 Aug 2021 05:00
URI: http://nbrc.sciencecentral.in/id/eprint/535

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