The interaction between compound 8b and BSA was also investigated.
The computational small molecule-protein docking analysis illustrated the possible interaction between compound 9 and RNA polymerase II.
Furthermore, docking studies revealed strong interaction between compound 4h and the key residues of BACE1 active site.
The interaction between compound 1b and copper surface was investigated using atomic force microscope (AFM) and X-ray photoelectron spectra (XPS).
Besides a pool of hydrophobic interaction between compound q1 and Phe97, Leu70, Ala172, Ile79, Leu158, Met174, Phe176, Ile54, Val35, Val27, Leu359 and Ala155 also stabilize the interaction (Fig. 5a).
Unfortunately, our study of the interaction between compound C and the Ndc80 complex has been complicated by the inability of the compound to enter cells.
This result indicated that there was an interaction between compound 4b and Fe3+ or Zn2+ ion due to complex formation.
A significant interaction between compound and EDL was observed for glycerol-3-phosphate dehydrogenase 1 (Gpd1) and FK506-binding protein 5 (Fkbp51), indicating that equipotent doses of the two pyrethroids did not elicit similar changes in expression at 6 h post-exposure.
According to the model, the benzofuran and isopropyl ester moieties do not significantly interact with the protein, with the closest distance between the benzofuran and Lys591 being 3.11 A and the closest distance between the isopropyl ester and Thr620 being 5.83 A. The binding score of –31.3 for compound 1 reflects the strong binding interaction between compound 1 and the STAT3 SH2 domain.
