ArticleThe Journal of chemical physics2013
Identification of small-molecule binding pockets in the soluble monomeric form of the Aβ42 peptide.
Article in The Journal of chemical physics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 84 citations in OpenAlex.
- Targeting protein disorder: the next hurdle in drug discovery.Nature reviews. Drug discovery · 2025Review
- Article
- Identification of Catechins' Binding Sites in Monomeric AInternational journal of molecular sciences · 2023Article
- A Small Molecule Stabilizes the Disordered Native State of the Alzheimer's Aβ Peptide.ACS chemical neuroscience · 2022Article
- Dynamics of Amyloid Formation from Simplified Representation to Atomistic Simulations.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Intrinsically disordered proteins and biomolecular condensates as drug targets.Current opinion in chemical biology · 2021Review
- Computational strategy for intrinsically disordered protein ligand design leads to the discovery of p53 transactivation domain I binding compounds that activate the p53 pathway.Chemical science · 2020Article
- Targeting Intrinsically Disordered Proteins through Dynamic Interactions.Biomolecules · 2020Review
- The Impact of Natural Compounds on S-Shaped Aβ42 Fibril: From Molecular Docking to Biophysical Characterization.International journal of molecular sciences · 2020Article
- Computer-Aided Drug Design of β-Secretase, γ-Secretase and Anti-Tau Inhibitors for the Discovery of Novel Alzheimer's Therapeutics.International journal of molecular sciences · 2020Review
- Novel Small Molecules Targeting the Intrinsically Disordered Structural Ensemble of α-Synuclein Protect Against Diverse α-Synuclein Mediated Dysfunctions.Scientific reports · 2019Article
- Modulation of Amyloid-β42 Conformation by Small Molecules Through Nonspecific Binding.Journal of chemical theory and computation · 2019Article
- Modulation of Disordered Proteins with a Focus on Neurodegenerative Diseases and Other Pathologies.International journal of molecular sciences · 2019Review
- Simulations of mutant p53 DNA binding domains reveal a novel druggable pocket.Nucleic acids research · 2019Article
- Conservation of Potentially Druggable Cavities in Intrinsically Disordered Proteins.ACS omega · 2018Article
- The Rational Discovery of a Tau Aggregation Inhibitor.Biochemistry · 2018Article
- Comparing the Aggregation Free Energy Landscapes of Amyloid Beta(1-42) and Amyloid Beta(1-40).Journal of the American Chemical Society · 2017Article
- Advantages of Structure-Based Drug Design Approaches in Neurological Disorders.Current neuropharmacology · 2017Review
- Nortriptyline inhibits aggregation and neurotoxicity of alpha-synuclein by enhancing reconfiguration of the monomeric form.Neurobiology of disease · 2017Article
- Methods of probing the interactions between small molecules and disordered proteins.Cellular and molecular life sciences : CMLS · 2017Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The aggregation of intrinsically disordered peptides and proteins is associated with a wide range of highly debilitating neurological and systemic disorders. In this work we explored the potential of a structure-based drug discovery procedure to target one such system, the soluble monomeric form of the Aβ42 peptide. We utilised for this purpose a set of structures of the Aβ42 peptide selected from clusters of conformations within an ensemble generated by molecular dynamics simulations. Using these structures we carried out fragment mapping calculations to identify binding "hot spots" on the monomeric form of the Aβ42 peptide. This procedure provided a set of hot spots with ligand efficiencies comparable to those observed for structured proteins, and clustered into binding pockets. Such binding pockets exhibited a propensity to bind small molecules known to interact with the Aβ42 peptide. Taken together these results provide an initial indication that fragment-based drug discovery may represent a potential therapeutic strategy for diseases associated with the aggregation of intrinsically disordered proteins.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.