Confinement physics of highly anisotropic supramolecular assemblies in thin liquid films: A perspective on amyloid fibrils
7 affiliations
- 1Jerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences
- 2Institute of Physical Chemistry
- 3Bulgarian Academy of Sciences
- 4Laboratory of Physics and Physical Chemistry of Foods
- 5Wageningen University
- 6Institute for Condensed Matter Physics
- 7Technical University of Darmstadt
Abstract
Amyloid fibrils derived from non-pathogenic proteins are among the most efficient protein-based stabilizers of foams and emulsions, yet the physicochemical basis of their colloidal performance remains incompletely understood. Substantial progress has been achieved in elucidating amyloidogenesis pathways, high-resolution fibril structures and the behaviour of fibrils at soft interfaces. Nevertheless, the physicochemical mechanisms through which fibril attributes and emergent interfacial self-organization are translated into macroscopic colloid stability remain fragmented and largely empirical. Here we propose a conceptual framework for advancing this problem. We argue that a major limitation arises from overlooking a decisive hierarchical level: the thin liquid film separating interacting foam bubbles or emulsion droplets. Such a film constitutes the physical locus where coalescence may be arrested through confinement-induced colloidal interactions leading to overall colloid stabilization. Beyond the problem of colloid stability, examination of such interactions in amyloid fibril-based systems exposes a broader physicochemical question concerning the behaviour of highly anisotropic supramolecular assemblies under film-confinement conditions. This Perspective identifies the principal knowledge gaps limiting mechanistic understanding of amyloid fibril-mediated colloid stabilization and discusses how its physicochemical description can be achieved through resolution of the identified knowledge gaps. We propose that amyloid fibrils should be viewed not only as high-performance colloidal stabilizers but also as experimentally mature model systems for exploring the confinement physics of highly anisotropic surface-active supramolecular entities.
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BibTeX
@misc{gochev2026confinement,
title = {{Confinement physics of highly anisotropic supramolecular assemblies in thin liquid films: A perspective on amyloid fibrils}},
author = {Georgi G. Gochev and Elena Mileva and Leonard M.C. Sagis and Reinhard Miller},
howpublished = {ChemRxiv},
year = {2026},
month = sep,
doi = {10.26434/chemrxiv.15008443/v1},
url = {https://chemrxiv.org/doi/full/10.26434/chemrxiv.15008443/v1},
note = {CC BY},
}
RIS
TY - UNPB
TI - Confinement physics of highly anisotropic supramolecular assemblies in thin liquid films: A perspective on amyloid fibrils
AU - Georgi G. Gochev
AU - Elena Mileva
AU - Leonard M.C. Sagis
AU - Reinhard Miller
PY - 2026
DA - 2026/09/07
PB - ChemRxiv
DO - 10.26434/chemrxiv.15008443/v1
UR - https://chemrxiv.org/doi/full/10.26434/chemrxiv.15008443/v1
AB - Amyloid fibrils derived from non-pathogenic proteins are among the most efficient protein-based stabilizers of foams and emulsions, yet the physicochemical basis of their colloidal performance remains incompletely understood. Substantial progress has been achieved in elucidating amyloidogenesis pathways, high-resolution fibril structures and the behaviour of fibrils at soft interfaces. Nevertheless, the physicochemical mechanisms through which fibril attributes and emergent interfacial self-organization are translated into macroscopic colloid stability remain fragmented and largely empirical. Here we propose a conceptual framework for advancing this problem. We argue that a major limitation arises from overlooking a decisive hierarchical level: the thin liquid film separating interacting foam bubbles or emulsion droplets. Such a film constitutes the physical locus where coalescence may be arrested through confinement-induced colloidal interactions leading to overall colloid stabilization. Beyond the problem of colloid stability, examination of such interactions in amyloid fibril-based systems exposes a broader physicochemical question concerning the behaviour of highly anisotropic supramolecular assemblies under film-confinement conditions. This Perspective identifies the principal knowledge gaps limiting mechanistic understanding of amyloid fibril-mediated colloid stabilization and discusses how its physicochemical description can be achieved through resolution of the identified knowledge gaps. We propose that amyloid fibrils should be viewed not only as high-performance colloidal stabilizers but also as experimentally mature model systems for exploring the confinement physics of highly anisotropic surface-active supramolecular entities.
ER -