ArticleThe journal of physical chemistry. B2022
Side Chain Geometry Determines the Fibrillation Propensity of a Minimal Two-Beads-per-Residue Peptide Model.
Article in The journal of physical chemistry. B, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- A Coarse-Grained MD Model for Disorder-To-Order Transitions in PolyQ Aggregation.Journal of chemical theory and computation · 2025Article
- Challenges in studying the liquid-to-solid phase transitions of proteins using computer simulations.Current opinion in chemical biology · 2023Review
- Modified Smoluchowski Rate Equations for Aggregation and Fragmentation in Finite Systems.The journal of physical chemistry. B · 2023Article
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2 authors.
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Abstract
The molecular mechanism of fibrillation is an important issue for understanding peptide aggregation. In our previous work, we demonstrated that the interchain attraction and intrachain bending stiffness control the aggregation kinetics and transient aggregate morphologies of a one-bead-per-residue implicit solvent peptide model. However, that model did not lead to fibrillation. In this work, we study the molecular origin of fibril formation using a two-beads-per-residue model, where one bead represents the backbone residue atoms and the other the side chain atoms. We show that the side chain geometry determines the fibrillation propensity that is further modulated by the modified terminal beads. This allows us to bring out the effects of side chain geometry and terminal capping on the fibrillation propensity. Our model does not assume a secondary structure and is, perhaps, the simplest bead-based chain model leading to fibrillation.
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