Assessing drug-protein binding by simulation of stereoselective energy transfer dynamics: electronic interactions between tryptophan and flurbiprofen
Document typeConference report
PublisherBarcelona Supercomputing Center
Rights accessOpen Access
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.
CitationPinheiro, Silvana; Curutchet, Carles. Assessing drug-protein binding by simulation of stereoselective energy transfer dynamics: electronic interactions between tryptophan and flurbiprofen. A: 3rd BSC International Doctoral Symposium. "Book of abstracts". Barcelona: Barcelona Supercomputing Center, 2015, p. 79-81.