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Updated: Sep 19, 2025
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Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils
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Lysozyme Amyloid Modulates Membrane Structure and Hydration and Impacts Its Fusogenicity
Shah Imtajul Haque1, Ria Saha1, Vibeizonuo Rupreo2
1Department of Chemical and Biological Sciences, S.N Bose National Centre for Basic Sciences, JD-Block, Sector-III, Salt Lake, Kolkata 700106, India.
Langmuir : the ACS Journal of Surfaces and Colloids
|June 18, 2025
Summary
Lysozyme amyloid fibrils disrupt cell membranes, impairing function. Ordered lipid membranes offer some protection against this amyloid-induced membrane damage.
Area of Science:
- Biochemistry
- Cell Biology
- Biophysics
Background:
- Lysozyme, prevalent in cells, can form cytotoxic amyloid fibrils under stress.
- Amyloid formation inactivates lysozyme and can disrupt cellular membrane functions.
Purpose of the Study:
- To investigate the interaction of lysozyme amyloid fibrils with different model lipid membranes.
- To understand how these interactions affect membrane properties and fusion propensity.
Main Methods:
- Dynamic light scattering
- Fluorescence spectroscopy
- Scanning electron microscopy
- THz-Fourier Transform Infrared Spectroscopy (FTIR)
Main Results:
- Lysozyme amyloids interact with and alter the ordering and hydration of lipid membranes.
- Liposome fusion propensity is significantly reduced in the presence of amyloid fibrils.
- Ordered, raft-like membranes show less reduction in fusion propensity compared to non-raft-like membranes.
Conclusions:
- Lysozyme amyloid fibrils pose a threat to membrane integrity and function.
- Membrane composition and order influence susceptibility to amyloid-induced damage, with raft-like membranes offering greater resilience.
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