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Modulation of Biomolecular Aggregate Morphology and Condensate Infectivity.

Josephine C Ferreon1, Kyoung-Jae Choi1, My Diem Quan1

  • 1Department of Biochemistry and Molecular Pharmacology, Baylor College of Medicine, Houston, TX 77030, USA.

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|May 4, 2026
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Summary
This summary is machine-generated.

Solution composition dictates protein aggregate structures in neurodegenerative diseases like Alzheimer's and ALS. These findings reveal how phase transitions influence pathological protein formations and their spread.

Keywords:
ALSAlzheimer’s diseaseFLIMLLPSaggregationbiomolecular condensatesfibrillationhnRNPA1phase transitionsprion-like domain

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Neuroscience

Background:

  • Neurodegenerative diseases are characterized by diverse protein aggregates, such as Lewy bodies in Alzheimer's disease (AD) and filaments in amyotrophic lateral sclerosis (ALS).
  • The physical mechanisms driving the varied morphologies of these pathological protein aggregates are not well understood.
  • The prion-like domain of hnRNPA1 (A1PrD) is implicated in AD and ALS.

Purpose of the Study:

  • To investigate how solution composition and phase transition dynamics influence the aggregation of the hnRNPA1 prion-like domain (A1PrD).
  • To understand the physical mechanisms behind the diverse pathological protein aggregate morphologies observed in neurodegenerative diseases.

Main Methods:

  • 3D timelapse microscopy
  • Fluorescence lifetime imaging microscopy
  • Analysis of A1PrD and RNA interactions

Main Results:

  • Solution conditions were shown to modulate phase separation, gelation, and fibrillation of A1PrD, leading to distinct structures (fibril, gel, starburst).
  • Interactions between A1PrD and RNA influenced the balance between pathological and physiological condensates.
  • Amyloid-rich starburst aggregates exhibited prion-like seeding capabilities toward amyloid-poor condensates.

Conclusions:

  • The interplay between solution composition and the kinetics of phase separation, gelation, and fibrillation governs the diverse pathological aggregate morphologies in neurodegenerative diseases.
  • Understanding these physical mechanisms is crucial for deciphering the progression of diseases like AD and ALS.