## 3 Results and Discussion
### Zw-Pes Membrane Models Interactions with Human Serum Proteins
\begin{table}
\begin{tabular}{c c c c} \hline \hline
**Ligand** & **Protein** & **Binding Energy** & \multicolumn{2}{c}{**Recceptor Contacts**} \\ \cline{3-4}  & & **(kcal/mol)** & **Hydrophilic** & **Hydrophobic** \\ \hline MMP–PES & HSA & \(-8.6\) & Leu115, His145, Ser193, Asp108 \({}^{a}\), & Tyr138, Ile142, Ala194, Pro147, \\  & & \(-8.6\) & Arg145 \({}^{a}\), Lys190, Glu141 \({}^{a}\), Arg186 & Leu463, Gln459, Asn109, Pro110, \\  & & & \({}^{a}\), Arg428 \({}^{a}\), Glu425 \({}^{b}\), Arg145 \({}^{b}\). & Ile523, Val424 \\ MMP–PES & FB & \(-6.6\) & Ser47, Arg 50 \({}^{a}\), Asp61 \({}^{a}\), Lys58 \({}^{a}\), & Cys28, Trp33, Cys49, Cys76, Val74, \\  & & & Lys29 \({}^{a}\), Asp61 \({}^{b}\), Arg50 \({}^{b}\). & Ala59, Pro70, Leu66, Ala68, Leu 72, \\  & & & Ser286, Lys276, Asp236 \({}^{a}\), Arg220 \({}^{a}\), & Phe211, His300, Phe285, Gln283, \\  & & & & Gly86, His207, His208 \\  & & & Arg186, Arg114, Arg117 \({}^{a}\), Lys137 & Leu141, Lys137, Tyr161, Leu182, \\  & & & Asp108 \({}^{b}\), His146 \({}^{b}\), Lys190 \({}^{b}\). & Gln459, Ala194, Pro110 \\  & & & & His207, Tyr238, Lys291, Lys276, \\  & & & & Gln92, Glu212 \({}^{a}\), Asp236 \({}^{a}\), Asp297 \\  & & & & Asp90 \({}^{b}\), Lys239 \({}^{b}\). & Ser298, Trp214 \({}^{c}\), \\  & & & & Lys293, Pro447, His288, Asp451 \({}^{c}\), Leu198, Pro339, Ala191, Val455, \\  & & & & Ser31, Asp61 \({}^{a}\), Lys29 \({}^{a}\), Arg50 \({}^{a}\), & Ala59, Pro70, Pro60, Trp33, Met51, \\  & & & & Asp61 \({}^{b}\), Arg50 \({}^{b}\), Ser47 \\  & & & & His300, Gln92, Tyr238, Glu212 \({}^{a}\), \\  & & & & Lys276 \({}^{a}\), Lys219 \({}^{a}\), Asp90 \({}^{b}\), & Tyr96, Gly86, Asp297 \({}^{c}\), Ser87, \\  & & & & His207 \({}^{b}\), Lys239 \({}^{b}\). & Phe211 \({}^{c}\). \\ \hline \hline \end{tabular} \({}^{a}\): Weak Van der Waals, \({}^{b}\): Attractive Charge, \({}^{c}\): Pi–P interactions.  
\end{table} 
Table 3: Binding energy results and receptor contacts of HSA, FB, and Tr interactions with MMP–PES, MPC–PES, and MBP–PES models. pocket, concluding MBP-PES model ligands are Tyr452, Val455, Ala191, Cys448, Trp214, Val293, Glu292, Pro447, His288, Asp451, Phe157, Leu198, Pro339, and Ser 192. According to the results shown in Figure 11a-c images, the zwitterion was bound to HSA via hydrogen bonding by interacting with Asn295, Arg218, Lys436, Glu292, Lys195, and Arg222. Nonspecific interactions like hydrophobic contacts and other electrostatic attractions could be distinguished between ligand and HSA protein. The binding energy of the PES model interaction with HSA was found to be \(-\)10.3 kcal/mol, and it was found to be \(-\)5.7 kcal/mol for the interaction between MBP and HSA. The binding energy of ZW-modified PES (MBP-PES) was found to be \(-\)8.5 kcal/mol, demonstrating the impact of ZW on the improvement of PES hemocompatibility (Table 3, entry 3). The interaction affinity energy of MBP-PES with FB and Tr was close to the MMP-PES ligand, which demonstrated that the n-Bu group has no significant influence in this study. In comparison, MBP-PES exhibited four hydrogen bonds with the active sites of HSA, while MPC-PES only showed two, which plays an important role in hemocompatibility. The stronger hydrogen shell of MBP-PES was, therefore, anticipated to make it a more compatible ligand. When MPC-PES was docked with HSA, it was found that this ligand had higher affinity energy (\(-\)9.2 kcal/mol) compared to MBP-PES as well as different protein-ligand interactions, which indicates that it is more likely to have fewer antifouling and hemocompatibility properties in experimental situations. This trend represents evidence when ligands were docked with FB and Tr, in both cases, MPC-PES showed an approximately 1 kcal/mol higher affinity energy than MBP-PES. Typically, zwitterionic materials display distinctive behaviors as a result of their dipole moments.