ArticleBioorganic & medicinal chemistry2009
Computational selection of inhibitors of Abeta aggregation and neuronal toxicity.
Article in Bioorganic & medicinal chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 37 citations in OpenAlex.
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- Changing Paradigm from one Target one Ligand Towards Multi-target Directed Ligand Design for Key Drug Targets of Alzheimer Disease: An Important Role of In Silico Methods in Multi-target Directed Ligands Design.Current neuropharmacology · 2018Article
- Computer Aided Drug Design and its Application to the Development of Potential Drugs for Neurodegenerative Disorders.Current neuropharmacology · 2018Review
- Alternative pre-approved and novel therapies for the treatment of anthrax.BMC infectious diseases · 2016Review
- Allosteric inhibitors of Coxsackie virus A24 RNA polymerase.Bioorganic & medicinal chemistry · 2016Article
- Disease-modifying anti-Alzheimer's drugs: inhibitors of human cholinesterases interfering with β-amyloid aggregation.CNS neuroscience & therapeutics · 2014Article
- Computational approaches to understanding protein aggregation in neurodegeneration.Journal of molecular cell biology · 2014Review
- Targeted studies on the interaction of nicotine and morin molecules with amyloid β-protein.Journal of molecular modeling · 2014Article
- The role of molecular simulations in the development of inhibitors of amyloid β-peptide aggregation for the treatment of Alzheimer's disease.ACS chemical neuroscience · 2012Review
- Pharmacophore selection and redesign of non-nucleotide inhibitors of anthrax edema factor.Toxins · 2012Review
- Structure-based redesign of an edema toxin inhibitor.Bioorganic & medicinal chemistry · 2012Article
- Transformation of amyloid β(1-40) oligomers into fibrils is characterized by a major change in secondary structure.Cellular and molecular life sciences : CMLS · 2011Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Alzheimer's disease (AD) is characterized by the cerebral accumulation of misfolded and aggregated amyloid-beta protein (Abeta). Disease symptoms can be alleviated, in vitro and in vivo, by 'beta-sheet breaker' pentapeptides that reduce plaque load. However the peptide nature of these compounds, made them biologically unstable and unable to penetrate membranes with high efficiency. The main goal of this study was to use computational methods to identify small molecule mimetics with better drug-like properties. For this purpose, the docked conformations of the active peptides were used to identify compounds with similar activities. A series of related beta-sheet breaker peptides were docked to solid state NMR structures of a fibrillar form of Abeta. The lowest energy conformations of the active peptides were used to design three dimensional (3D)-pharmacophores, suitable for screening the NCI database with Unity. Small molecular weight compounds with physicochemical features and a conformation similar to the active peptides were selected, ranked by docking and biochemical parameters. Of 16 diverse compounds selected for experimental screening, 2 prevented and reversed Abeta aggregation at 2-3microM concentration, as measured by Thioflavin T (ThT) fluorescence and ELISA assays. They also prevented the toxic effects of aggregated Abeta on neuroblastoma cells. Their low molecular weight and aqueous solubility makes them promising lead compounds for treating AD.
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Registered trials
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