Molecular Dynamic Studies of the Complex Polyethylenimine and Glucose Oxidase
Szefler, B; Diudea, MV; Putz, MV; Grudzinski, IP
| HERO ID | 4314415 |
|---|---|
| In Press | No |
| Year | 2016 |
| Title | Molecular Dynamic Studies of the Complex Polyethylenimine and Glucose Oxidase |
| Authors | Szefler, B; Diudea, MV; Putz, MV; Grudzinski, IP |
| Journal | International Journal of Molecular Sciences |
| Volume | 17 |
| Issue | 11 |
| Abstract | Glucose oxidase (GOx) is an enzyme produced by Aspergillus, Penicillium and other fungi species. It catalyzes the oxidation of β-d-glucose (by the molecular oxygen or other molecules, like quinones, in a higher oxidation state) to form d-glucono-1,5-lactone, which hydrolyses spontaneously to produce gluconic acid. A coproduct of this enzymatic reaction is hydrogen peroxide (H₂O₂). GOx has found several commercial applications in chemical and pharmaceutical industries including novel biosensors that use the immobilized enzyme on different nanomaterials and/or polymers such as polyethylenimine (PEI). The problem of GOx immobilization on PEI is retaining the enzyme native activity despite its immobilization onto the polymer surface. Therefore, the molecular dynamic (MD) study of the PEI ligand (C14N8_07_B22) and the GOx enzyme (3QVR) was performed to examine the final complex PEI-GOx stabilization and the affinity of the PEI ligand to the docking sites of the GOx enzyme. The docking procedure showed two places/regions of major interaction of the protein with the polymer PEI: (LIG1) of -5.8 kcal/mol and (LIG2) of -4.5 kcal/mol located inside the enzyme and on its surface, respectively. The values of enthalpy for the PEI-enzyme complex, located inside of the protein (LIG1) and on its surface (LIG2) were computed. Docking also discovered domains of the GOx protein that exhibit no interactions with the ligand or have even repulsive characteristics. The structural data clearly indicate some differences in the ligand PEI behavior bound at the two places/regions of glucose oxidase. |
| Doi | 10.3390/ijms17111796 |
| Pmid | 27801788 |
| Wosid | WOS:000388809600030 |
| Is Certified Translation | No |
| Dupe Override | No |
| Is Public | Yes |
| Language Text | English |