## 3 Results and Discussion
### Zw-Pes Membrane Models Interactions with Human Serum Proteins  
This computational study has been extended to examine the interactions between MBP-PES, MMP-PES, and MPC-PES membrane models (Figure 8) with HSA, FB, and Tr to evaluate the impact of these ZWs with the opposite dipole orientation on the membrane hemocompatibility. Data from docking studies showed that the MPC-PES model had a  
Figure 7: (**a**) 2D interaction diagrams, (**b**) 3D images of docking MBP ligand–protein interactions, and (**c**) electrostatic maps of interactions. higher binding affinity than the MBP-PES and the MMP-PES models, as well as different interaction patterns for each of the proteins (Figures 9-11 and Table 3). When ZW-PES membrane models docked into the protein active sites, two significant interactions were observed: (1) polar interactions induced by ZW and SO\({}_{2}\) groups and (2) hydrophobic interactions caused by protein chains with the PES membrane. Figure 9: Molecular docking of the interaction between the HSA, FB, and TR proteins and the MMP-PES ligand; (**a**) 3D images, (**b**) 2D interaction diagrams, and (**c**) 3D docking poses with ball–stick figures indicating polar interactions with important contributing amino acids (Draw by Discovery Studio Visualizer). Figure 10: _Cont._  
Figure 11: _Cont._  
Figure 10: Molecular docking of the interaction between the HSA, FB, and TR proteins and the MPC–PES ligand; (**a**) 3D images, (**b**) 2D interaction diagrams, and (**c**) 3D docking poses with ball–stick figures indicating polar interactions with important contributing amino acids (Draw by Discovery Studio Visualizer). Figure 11: Molecular docking of the interaction between the HSA, FB, and TR proteins and the MBP-PES ligand; **(a)** 3D images, **(b)** 2D interaction diagrams, and **(c)** 3D docking poses with ball–stick figures indicating polar interactions with important contributing amino acids (Draw by Discovery Studio Visualizer). According to the docking result of the MMP-PES model with HSA protein (Figure 9), Leu115, His145, Ser193, Asp108, Pro110, Ile523, and Arg145 are amino acids involved in hydrophilic interactions. While, in hydrophobic interactions, Tyr138, Ile142, Ala194, Pro147, Leu463, Gln459, Asn109, Pro110, Ile 523, and Val424 were responsible residues. MMP showed a potentially positive effect on the antifouling property of PES by reducing the interaction affinity energy to \(-8.6\) kcal/mol with HSA protein (Table 3, entry 1), compared to the interaction affinity energy of \(-10.3\) kcal/mol between PES ligand and HSA protein (Table 1, entry 1). On the other hand, MPC-PES docking into the HSA active site also revealed hydrophobic and hydrophilic interactions as the main interactions between protein and ligand. The Lys137, Leu115, Ile142, Tyr138, Met123, Clu141, Lys137, Tyr161, Leu182, Asn109, Leu463, Val462, Pro147, Gln459, Ala194, and Pro110 amino acids were expected to have hydrophobic contact with MPC-PES, while Arg186, Arg114, Lys137, Ser193, Arg117, Arg197, and Arg145 were responsible for the formation of hydrogen bonds, and Asp108, His146, and Lys190 were involved in attractive charge interactions as polar contacts (Figure 10). The binding energy values of MPC-PES with all the examined proteins were in the range between the binding energy values of interaction between PES and MPC alone, indicating that even though MPC structure had a significant effect on PES hemocompatibility improvement, it was not as much as MPC alone because of PES hydrophobic interactions. As shown in Figure 11a-c images, docking studies were also performed on MBP-PES with HSA to explore the potential impact of the n-Bu group and the impact of dipole orientation as a key feature of ZW chains on PES hemocompatibility. Docking simulation with the HSA protein and MBP-PES chain showed the residues responsible for hydrophobic