Assessing drug-protein binding by simulation of stereoselective energy transfer dynamics: electronic interactions between tryptophan and flurbiprofen

Protein fluorescence decays are difficult to interpret and often involving several energy transfer processes among Trp residues or Trp-ligands. In this study, we simulate EET rates by computing MD-averaged electronic couplings V. Fluorescence decays have been observed for the HSA protein bound to the S and R enantiomers of FBP. So far, our results in the HSA-FBP system agree with the experimental hypothesis (stereoselective energy transfer) and strongly support the binding modes proposed for the R and S enantiomers in HSA