Article

Energetic profiling reveals thermodynamic principles underlying amyloid fibril maturation

2025-05-16

Abstract excerpt

Amyloid fibrils adopt diverse structural polymorphs that underlie disease-specific phenotypes, but the thermodynamic principles guiding their formation and maturation remain poorly understood. Here, we apply energetic profiling to structural time series from cryo-EM datasets of IAPP, tau, and α-synuclein to decode the principles governing fibril maturation, stability and polymorphic divergence. By mapping residue-...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 4b63df86-fad7-5100-9daf-c34848aa378c
DOI: 10.1101/2025.05.14.653959

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Energetic profiling reveals thermodynamic principles underlying amyloid fibril maturationDOI 10.1101/2025.05.14.653959Read

CryoPhold: CryoEM meets AlphaFold and molecular simulation to reveal protein dynamicsSemantic proximity Read

How is the Amyloid Fold Built? Polymorphism and the Microscopic Mechanisms of Fibril AssemblySemantic proximity Read

To What Extent is Anfinsen’s Thermodynamic Hypothesis Consistent With the Formation and Polymorphism of Amyloid Fibrils?Semantic proximity Read

Amyloid assembly is dominated by misregistered kinetic traps on an unbiased energy landscape.Semantic proximity Read

Examining the Ensembles of Amyloid- <i>β</i> Monomer Variants and their Propensities to Form Fibers Using an Energy Landscape Visualization MethodSemantic proximity Read

Exploring the aggregation free energy landscape of the amyloid-β protein (1-40).Semantic proximity Read

Diverging co-translational protein complex assembly pathways are governed by interface energy distributionSemantic proximity Read

Polymorphic structures of Alzheimer's β-amyloid globulomers.Semantic proximity Read

Multiscale simulations reveal the driving forces underlying V337M-induced tau core fragment aggregation.Semantic proximity Read

Conformational ensembles of the human intrinsically disordered proteome: Bridging chain compaction with function and sequence conservationSemantic proximity Read

Reconstitution of the Alzheimer’s Disease Tau Core Structure from Recombinant Tau 297–391 Yields Variable Quaternary Structures as Seen by Negative Stain and Cryo-EMSemantic proximity Read

Massively parallel genetic perturbation reveals the energetic architecture of an amyloid beta nucleation reactionSemantic proximity Read