Fig. 7
ODSH binds to HMGB1 and induces conformational changes on HMGB1. The localized surface plasmon resonance (LSPR) binding efficiency of ODSH to HMGB1 was determined by applying ODSH at 1 and 10 µg/mL and measuring its ability to bind to carboxyl sensor chips coated with recombinant HMGB1. A The representative kinetic binding curves demonstrating the ability of ODSH to associate and then dissociate off of HMGB1. The kinetic binding curves were then used to compute the bind efficiency (KD) for ODSH to HMGB1. Next, induced fit docking experiment was conducted to determine the interactions of ODSH with the B-Box domain of HMGB1 B Surface representation of HMGB1 with ODSH bound to the B-Box domain wherein the blue region represents the concentration of negatively charged, red for positively charged and grey for neutral amino acid residues. ODSH is represented in CPK form with the spheres following the same color pattern as the surface of protein. C The representative 3D docking pose of ODSH bound to HMGB1 B-Box domain. D Superimposition of native, energy minimized HMGB1 (red ribbons) and ODSH docked to HMGB1 (green ribbons). C and D ODSH was represented as ball and stick model whereas the amino acids are shown as thin tubes with atom colors shown as orange for carbons of ODSH, red for oxygen, blue for nitrogen, yellow for sulfur, and grey for carbons belonging to the amino acid residues of ODSH bound HMGB1 and yellow for carbons belonging to the amino acids of native HMGB1. Dashed black lines represent hydrogen bonds and dashed red lines represent ionic interactions between ODSH and HMGB1