Identification of Amyloid Regions and Mechanisms from Sequence-Based Modeling and Molecular Dynamics Simulation: A Case Study of the Intrinsically Disordered Protein DPF3
) congruently underscored its inability to maintain a steric zipper configuration and nucleate into oligomers enriched in β character. Using only the sequence of a target protein as starting input, our methodology noteworthily proved to be reliable for detecting aggregation-prone regions, assessing their amyloidogenicity, and elucidating their fibrillation mechanisms while holding promise for the design of new anti-amyloid drugs and amyloid-inspired biomaterials.
Authors
- Julien Mignon (ORCID: https://orcid.org/0000-0003-1223-4501)
- Catherine Michaux (ORCID: https://orcid.org/0000-0001-8208-3310)
- Hugo Bâlon
- Antonio Monari (ORCID: https://orcid.org/0000-0001-9464-1463)
- Tanguy Leyder
- Denis Mottet (ORCID: https://orcid.org/0000-0001-5410-1593)
Institutions
- Centre National de la Recherche Scientifique (FR)
- University of Namur (BE)
- University of Liège (BE)
- Université Paris Cité (FR)
- Interfaces Traitements Organisation et Dynamique des Systèmes (FR)
Publication Details
- Journal
- Journal of Chemical Information and Modeling
- Published
- 2026-04-16
- DOI
- https://doi.org/10.1021/acs.jcim.6c00951
- Primary Topic
- Alzheimer's disease research and treatments
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- Agence Nationale de la Recherche
- Fonds De La Recherche Scientifique - FNRS
- Commissariat Général à l'Investissement
- Fonds pour la Formation à la Recherche dans l’Industrie et dans l’Agriculture