Molecular dynamics simulations of Ibuprofen binding to Abeta peptides.

Abstract

Using replica exchange molecular dynamics simulations and the implicit solvent model we probed binding of ibuprofen to Abeta(10-40) monomers and amyloid fibrils. We found that the concave (CV) fibril edge has significantly higher binding affinity for ibuprofen than the convex edge. Furthermore, binding of ibuprofen to Abeta monomers, as compared to fibrils… (More)
DOI: 10.1016/j.bpj.2009.07.032

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Cite this paper

@article{Raman2009MolecularDS, title={Molecular dynamics simulations of Ibuprofen binding to Abeta peptides.}, author={E. Prabhu Raman and Takako Takeda and Dmitri K Klimov}, journal={Biophysical journal}, year={2009}, volume={97 7}, pages={2070-9} }