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Technique for Intranasal Administration of α-Synuclein Aggregates

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Alpha-synuclein-decorated nanoconjugates targeting alpha-synuclein assembly.

Marco Carrello¹, Filippo Busatta¹, Francisco Ramos-Martín²

¹Department of Biotechnology, University of Verona, Strada Le Grazie 15, 37134, Verona, Italy.

International Journal of Biological Macromolecules

|July 13, 2026

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Protein-functionalized nanoparticles (NPs) modulate alpha-synuclein (αS) aggregation, a key process in Parkinson's disease. Site-specific attachment of αS to NPs influences its assembly, offering new tools for neurodegenerative disease research.

Area of Science:

Neuroscience
Biochemistry
Nanotechnology

Background:

Alpha-synuclein (αS) aggregation is central to synucleinopathies like Parkinson's disease.
The intrinsically disordered nature of αS complicates its study and therapeutic targeting.
Protein-functionalized nanoparticles (NPs) offer a novel approach to modulate protein assembly.

Purpose of the Study:

To investigate the use of protein-functionalized NPs for modulating and probing αS assembly pathways.
To explore the impact of conjugation site on NP-αS interactions and αS aggregation.
To assess the potential of these nanoconjugates as tools for neurodegenerative disease research.

Main Methods:

Designed three nanoconjugates by attaching single-cysteine αS variants (at positions 18, 76, 140) to PEG-coated silica NPs.

Keywords:

Alpha-synuclein Nanoconjugate protein aggregation

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Assessed nanoconjugate properties including disorder preservation, cytotoxicity, and cellular uptake.

Evaluated effects on αS aggregation, tau protein aggregation, condensate formation, and lipid membrane interactions.

Main Results:

Nanoconjugates preserved αS disorder, showed low cytotoxicity, and were internalized by neuronal cells.
Site-specific conjugation influenced αS aggregation: NP-αS^A76C delayed fibril formation and inhibited tau aggregation, while NP-αS^A18C accelerated aggregation.
All nanoconjugates interacted with αS condensates and model lipid membranes, with conjugation position affecting NP-protein interactions.

Conclusions:

αS-functionalized NPs can modulate protein aggregation and condensate interactions with context-dependent site specificity.
The conjugation position is critical for tuning NP-protein interactions.
These nanoconjugates show promise for investigating and modulating pathological protein assembly in neurodegenerative diseases.