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Fluorogenic Hyaluronan Nanogels Track Individual Early Protein Aggregates Originated under Oxidative Stress. | LitMetric

AI Article Synopsis

  • Proteins are essential biomolecules whose functions depend on their correct folding; misfolding can lead to harmful aggregates and phase condensates.
  • The study introduces HA-RB, a special fluorescent compound that binds to early aggregates of a specific model protein (AtGAPC1), making them easier to visualize.
  • Using advanced imaging techniques, researchers demonstrate that HA-RB can effectively track these early protein aggregates, offering detailed insights into their formation dynamics with high precision in time and size.

Article Abstract

Proteins are broadly versatile biochemical materials, whose functionality is tightly related to their folding state. Native folding can be lost to yield misfolded conformations, often leading to formation of protein oligomers, aggregates, and biomolecular phase condensates. The fluorogenic hyaluronan HA-RB, a nonsulfonated glycosaminoglycan with a combination of polyanionic character and of hydrophobic spots due to rhodamine B dyes, binds to early aggregates of the model protein cytoplasmic glyceraldehyde-3-phosphate dehydrogenase 1 from (AtGAPC1) since the very onset of the oligomeric phase, making them brightly fluorescent. This initial step of aggregation has, until now, remained elusive with other fluorescence- or scattering-based techniques. The information gathered from nanotracking (via light-sheet fluorescence microscopy) and from FCS in a confocal microscope converges to highlight the ability of HA-RB to bind protein aggregates from the very early steps of aggregation and with high affinity. Altogether, this fluorescence-based approach allows one to monitor and track individual early AtGAPC1 aggregates in the size range from 10 to 100 nm with high time (∼10-2 s) and space (∼250 nm) resolution.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10811615PMC
http://dx.doi.org/10.1021/acsami.3c13202DOI Listing

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