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Phase Diagram Characterization Using Magnetic Beads as Liquid Carriers

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Competition Between Liquid-Liquid Crystalline Phase Separation (LLCPS) and Liquid-Liquid Phase Separation (LLPS) in

Milad Radiom¹, Raffaele Mezzenga¹

¹Department of Health Sciences and Technology, ETH Zürich, Zürich, 8092, Switzerland.

Advanced Science (Weinheim, Baden-Wurttemberg, Germany)

|January 28, 2026

Summary

Amyloid fibrils primarily form liquid-liquid crystalline phase separation (LLCPS), but pH changes can induce liquid-liquid phase separation (LLPS). This study clarifies amyloid fibril organization and control.

Keywords:

LLCPS LLPS amyloid fibrils condensates liquid crystals phase diagram phase transition

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Area of Science:

Colloidal physics
Biophysics
Materials science

Background:

Amyloid fibrils are protein aggregates forming condensed phases in biological systems and disease.
Two main separation pathways, liquid-liquid phase separation (LLPS) and liquid-liquid crystalline phase separation (LLCPS), can form these phases.
The interplay between LLPS and LLCPS in amyloid fibril dispersions is not fully understood.

Purpose of the Study:

To investigate the dominant phase separation pathway in amyloid fibril dispersions.
To determine the influence of solution conditions, specifically pH, on amyloid fibril phase behavior.
To establish a framework for controlling the organization of amyloid fibrils.

Main Methods:

Studied lysozyme and β-lactoglobulin amyloid fibrils.
Investigated phase separation behavior across a range of pH conditions.
Analyzed the formation of nematic condensates and their order.

Main Results:

Amyloid fibrils predominantly undergo LLCPS.
Increasing pH triggers a transition from LLCPS to LLPS.
Near the isoelectric point, condensates form without coherent nematic order, indicating a pH-dependent shift in dominant separation pathway.
Enthalpic attraction dominates over entropic ordering at low charge densities.

Conclusions:

LLCPS and LLPS in amyloid fibrils are distinct and separable processes.
Solution pH is a critical factor in controlling amyloid fibril organization.
Understanding the competition between LLCPS and LLPS can elucidate in vivo fibril organization and guide the design of amyloid-based materials.