ArticleThe journal of physical chemistry. B2026
The Monomeric Conformational Ensembles of Aβ40 and Aβ42 Encode Their Differential Amyloid Aggregation Propensity.
Article in The journal of physical chemistry. B, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Aβ40 and Aβ42 peptides differ by just two C-terminal residues, yet they display strikingly different aggregation and toxicity profiles. Whether this distinction is already encoded at the monomer level is still under debate. Here, we combine extensive all-atom simulations in explicit solvent, well-tempered metadynamics, and a tailored consensus cluster analysis to compare the monomeric ensembles of the two isoforms under identical conditions. Both peptides populate broad, coil-like conformational distributions; however, Aβ42 shows a systematically higher β-structure propensity, especially in the C-terminal region, and samples more extended conformations with higher hydrophobic exposure compared to Aβ40. These results support a mechanistic link between sequence-encoded monomer conformational preferences and the differential amyloidogenicity of the two isoforms, highlighting monomer-level determinants of Aβ42's distinct aggregation behavior.
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