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Fluorogenic Hyaluronan Nanogels Track Individual Early Protein Aggregates Originated under Oxidative Stress
Matteo Cingolani1, Francesca Lugli1, Mirko Zaffagnini2
1Dipartimento di Chimica "Giacomo Ciamician", Università di Bologna, 40126 Bologna, Italy.
ACS Applied Materials & Interfaces
|January 9, 2024
Summary
Hyaluronan HA-RB binds early protein aggregates, like those of Arabidopsis thaliana GAPC1, making them fluorescent. This novel method tracks small protein aggregates (10-100 nm) with high resolution.
Area of Science:
- Biochemistry
- Biophysics
- Molecular Biology
Background:
- Protein functionality depends on correct folding; misfolding leads to aggregates.
- Early protein aggregation stages are difficult to detect with existing methods.
Purpose of the Study:
- To develop a sensitive fluorescence-based method to detect and track early protein aggregation.
- To characterize the binding of hyaluronan HA-RB to early protein aggregates.
Main Methods:
- Utilized a fluorogenic hyaluronan probe (HA-RB) with polyanionic and hydrophobic properties.
- Employed nanotracking via light-sheet fluorescence microscopy and fluorescence correlation spectroscopy (FCS).
Main Results:
- HA-RB binds to early aggregates of Arabidopsis thaliana GAPC1 (AtGAPC1) at the onset of oligomerization.
- The probe enables bright fluorescence detection of these initial aggregates.
- High-affinity binding and tracking of individual AtGAPC1 aggregates (10-100 nm) were achieved with high temporal and spatial resolution.
Conclusions:
- HA-RB is a valuable tool for detecting and monitoring early protein aggregation events.
- This fluorescence-based approach overcomes limitations of previous techniques for studying initial aggregation steps.
