LIN5001 pulled out of the binding with T-A-K

We devised a minimal model of an LIN5001 binding site on a prion fibril that captures the main interactions at the atomic level of detail. The model consisted of eight 3-residue peptides (S-A-K) arranged in a parallel in-register β-sheet. The LIN5001 were docked manually. The simulation shows LIN5001 is pulled out of the binding site at a constant rate.

Publication Link: 
Structure-based drug design identifies polythiophenes as antiprion compounds
Link to video file: 
Herrman-etal_LCP_2015_2.mp4