ArticlePloS one2018
Etersalate prevents the formations of 6Aβ16-22 oligomer: An in silico study.
Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- The F19W mutation reduces the binding affinity of the transmembrane AβRSC advances · 2021Article
- Article
- C-Terminal Plays as the Possible Nucleation of the Self-Aggregation of the S-Shape AβACS omega · 2019Article
- Adequate prediction for inhibitor affinity of AβRSC advances · 2019Article
- Atomistic investigation of an Iowa Amyloid-β trimer in aqueous solution.RSC advances · 2018Article
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Authors and funding
5 authors.
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Abstract
Oligomerization of amyloid beta (Aβ) peptides has been considered as the crucially causative agent in the development of Alzheimer's disease. Etersalate, a nonsteroidal anti-inflammatory oral drug (United State Food and Drug Administration-Unique Ingredient Identifier: 653GN04T2G) was previously suggested to bind well to proto-fibrils of Aβ peptides in silico. Here, the effect of etersalate on the oligomerization of soluble Aβ16-22 hexamer (6Aβ16-22) were extensively investigated using temperature replica exchange molecular dynamics (REMD) simulations over ~16.8 μs in total for 48 replicas (350 ns per replica). The results reveal that etersalate can enter the inner space or bind on the surface of 6Aβ16-22 conformations, which destabilizes the hexamer. Etersalate was predicted to able to cross the blood brain barrier using prediction of absorption, distribution, metabolism, and excretion-toxicity (preADMET) tools. Overall, although the investigation was performed with the low concentration of trial inhibitor, the obtained results indicate that etersalate is a potential drug candidate for AD through inhibiting formation of Aβ oligomers with the average binding free energy of -11.7 kcal/mol.
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