Ontology highlight
ABSTRACT:
SUBMITTER: Raman EP
PROVIDER: S-EPMC2756381 | biostudies-literature | 2009 Oct
REPOSITORIES: biostudies-literature
Raman E Prabhu EP Takeda Takako T Klimov Dmitri K DK
Biophysical journal 20091001 7
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, results in a smaller free energy gain. The difference in binding free energies is likely to be related to the presence of the groove on the ...[more]