Nanoplatforms Targeting Intrinsically Disordered Protein Aggregation for Translational Neuroscience Applications DOI Creative Commons
Chih Hung Lo,

Lenny Yi Tong Cheong,

Jialiu Zeng

и другие.

Nanomaterials, Год журнала: 2025, Номер 15(10), С. 704 - 704

Опубликована: Май 8, 2025

Intrinsically disordered proteins (IDPs), such as tau, beta-amyloid (Aβ), and alpha-synuclein (αSyn), are prone to misfolding, resulting in pathological aggregation propagation that drive neurodegenerative diseases, including Alzheimer’s disease (AD), frontotemporal dementia (FTD), Parkinson’s (PD). Misfolded IDPs aggregate into oligomers fibrils, exacerbating progression by disrupting cellular functions the central nervous system, triggering neuroinflammation neurodegeneration. Furthermore, aggregated exhibit prion-like behavior, acting seeds released extracellular space, taken up neighboring cells, have a propagating pathology across different regions of brain. Conventional inhibitors, small molecules, peptides, antibodies, face challenges stability blood–brain barrier penetration, limiting their efficacy. In recent years, nanotechnology-based strategies, multifunctional nanoplatforms or nanoparticles, emerged promising tools address these challenges. These leverage tailored designs prevent remodel reduce associated neurotoxicity. This review discusses advances designed target Aβ, αSyn aggregation, with focus on roles reducing We examine critical aspects nanoplatform design, choice material backbone targeting moieties, which influence interactions IDPs. also highlight key mechanisms interaction between inhibit redirect cascade towards nontoxic, off-pathway species, disrupt fibrillar structures soluble forms. further outline future directions for enhancing IDP clearance, achieving spatiotemporal control, improving cell-specific targeting. nanomedicine strategies offer compelling paths forward developing more effective targeted therapies diseases.

Язык: Английский

Nanoplatforms Targeting Intrinsically Disordered Protein Aggregation for Translational Neuroscience Applications DOI Creative Commons
Chih Hung Lo,

Lenny Yi Tong Cheong,

Jialiu Zeng

и другие.

Nanomaterials, Год журнала: 2025, Номер 15(10), С. 704 - 704

Опубликована: Май 8, 2025

Intrinsically disordered proteins (IDPs), such as tau, beta-amyloid (Aβ), and alpha-synuclein (αSyn), are prone to misfolding, resulting in pathological aggregation propagation that drive neurodegenerative diseases, including Alzheimer’s disease (AD), frontotemporal dementia (FTD), Parkinson’s (PD). Misfolded IDPs aggregate into oligomers fibrils, exacerbating progression by disrupting cellular functions the central nervous system, triggering neuroinflammation neurodegeneration. Furthermore, aggregated exhibit prion-like behavior, acting seeds released extracellular space, taken up neighboring cells, have a propagating pathology across different regions of brain. Conventional inhibitors, small molecules, peptides, antibodies, face challenges stability blood–brain barrier penetration, limiting their efficacy. In recent years, nanotechnology-based strategies, multifunctional nanoplatforms or nanoparticles, emerged promising tools address these challenges. These leverage tailored designs prevent remodel reduce associated neurotoxicity. This review discusses advances designed target Aβ, αSyn aggregation, with focus on roles reducing We examine critical aspects nanoplatform design, choice material backbone targeting moieties, which influence interactions IDPs. also highlight key mechanisms interaction between inhibit redirect cascade towards nontoxic, off-pathway species, disrupt fibrillar structures soluble forms. further outline future directions for enhancing IDP clearance, achieving spatiotemporal control, improving cell-specific targeting. nanomedicine strategies offer compelling paths forward developing more effective targeted therapies diseases.

Язык: Английский

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