ArticleBiophysics and physicobiology2026
A lattice Monte Carlo model for amyloid fibril formation.
Article in Biophysics and physicobiology, 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
Proteins can aggregate to form amyloid fibrils, which are associated with a group of diseases collectively known as amyloidoses. Molecular dynamics simulations are widely used to study protein aggregation; however, it remains computationally challenging to investigate the entire aggregation process, from initial nucleation to the formation of mature amyloid fibrils, within a single simulation. In this study, we propose a Monte Carlo simulation based on a mathematical lattice model in which proteins are represented as spheres on a lattice. Motivated by the role of intramolecular β-sheet structures in accelerating aggregation, we classify protein states into three categories: monomer, intermediate possessing an intramolecular β-sheet structure, and fibril. By tuning the monomer-to-intermediate transition probability
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