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Updated: Mar 11, 2026

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
Published on: March 21, 2025
The multiple assemblies of VDAC: from conformational heterogeneity to β-aggregation and amyloid formation
Alexandre Boulbrima1, Davina Temple1, Georgios Psakis1
1School of Applied Sciences, Department of Biological Sciences, University of Huddersfield, Queensgate, Huddersfield HD1 3DH, U.K.
Abstract:
From their cellular localisation, to their atomic structure and their involvement in mitochondrial-driven cell death, voltage-dependent anion channels (VDACs) have challenged the scientific community with enigmas and paradoxes for over four decades. VDACs form active monomer channels in lipid bilayers, but they can also organise in multimeric assemblies. What induces, regulates and/or controls the monomer-multimer dynamics at the cellular level is not known. However, these state transitions appear to be relevant for mitochondria in making life or death decisions and for driving developmental processes. This review starts with a general introduction on VDACs and continues by examining VDAC oligomerisation/aggregation in light of recent discussions on VDAC-β-amyloid interactions and their involvement in Alzheimer's disease.
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