ArticleThe Journal of biological chemistry2011
Disordered binding of small molecules to Aβ(12-28).
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 49 citations in OpenAlex.
- Amodiaquine Modulates Aggregation and Disassembly of Amyloid-β and Tau and Attenuates Neuroinflammatory Responses and Aβ Production.Pharmaceutics · 2025Article
- Disrupting Amyloid Filaments of Tau by Means of Electric Fields.The journal of physical chemistry. B · 2025Article
- IDRdecoder: a machine learning approach for rational drug discovery toward intrinsically disordered regions.Frontiers in bioinformatics · 2025Article
- Chemical tools for study and modulation of biomolecular phase transitions.Chemical science · 2022Review
- Molecular Basis of Small-Molecule Binding to α-Synuclein.Journal of the American Chemical Society · 2022Article
- p27Cells · 2021Review
- Naphthoquinone Tryptophan Hybrids: A Promising Small Molecule Scaffold for Mitigating Aggregation of Amyloidogenic Proteins and Peptides.Frontiers in cell and developmental biology · 2019Review
- The ATAD2 bromodomain binds different acetylation marks on the histone H4 in similar fuzzy complexes.The Journal of biological chemistry · 2017Article
- A Small Molecule Causes a Population Shift in the Conformational Landscape of an Intrinsically Disordered Protein.Journal of the American Chemical Society · 2017Article
- Methods of probing the interactions between small molecules and disordered proteins.Cellular and molecular life sciences : CMLS · 2017Review
- Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell.Chemical reviews · 2016Review
- Dynamic Protein Interaction Networks and New Structural Paradigms in Signaling.Chemical reviews · 2016Review
- Induced Dipole-Dipole Interactions Influence the Unfolding Pathways of Wild-Type and Mutant Amyloid β-Peptides.The journal of physical chemistry. B · 2015Article
- Discovery of Small Molecules that Inhibit the Disordered Protein, p27(Kip1).Scientific reports · 2015Article
- Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Chemical reviews · 2015Review
- Atomic and dynamic insights into the beneficial effect of the 1,4-naphthoquinon-2-yl-L-tryptophan inhibitor on Alzheimer's Aβ1-42 dimer in terms of aggregation and toxicity.ACS chemical neuroscience · 2014Article
- Effects of Zn2+ binding on the structural and dynamic properties of amyloid β peptide associated with Alzheimer's disease: Asp1 or Glu11?ACS chemical neuroscience · 2013Article
- Identification of small-molecule binding pockets in the soluble monomeric form of the Aβ42 peptide.The Journal of chemical physics · 2013Article
- Temperature dependence of Congo red binding to amyloid β12-28.European biophysics journal : EBJ · 2013Article
- Molecular interactions of Alzheimer's biomarker FDDNP with Aβ peptide.Biophysical journal · 2012Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In recent years, an increasing number of small molecules and short peptides have been identified that interfere with aggregation and/or oligomerization of the Alzheimer β-amyloid peptide (Aβ). Many of them possess aromatic moieties, suggesting a dominant role for those in interacting with Aβ along various stages of the aggregation process. In this study, we attempt to elucidate whether interactions of such aromatic inhibitors with monomeric Aβ(12-28) point to a common mechanism of action by performing atomistic molecular dynamics simulations at equilibrium. Our results suggest that, independently of the presence of inhibitors, monomeric Aβ(12-28) populates a partially collapsed ensemble that is largely devoid of canonical secondary structure at 300 K and neutral pH. The small molecules have different affinities for Aβ(12-28) that can be partially rationalized by the balance of aromatic and charged moieties constituting the molecules. There are no predominant binding modes, although aggregation inhibitors preferentially interact with the N-terminal portion of the fragment (residues 13-20). Analysis of the free energy landscape of Aβ(12-28) reveals differences highlighted by altered populations of a looplike conformer in the presence of inhibitors. We conclude that intrinsic disorder of Aβ persists at the level of binding small molecules and that inhibitors can significantly alter properties of monomeric Aβ via multiple routes of differing specificity.
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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.