6533b824fe1ef96bd12814ee
RESEARCH PRODUCT
Kinetic and thermodynamic insights into interaction of erlotinib with epidermal growth factor receptor: Surface plasmon resonance and molecular docking approaches.
Saeideh Mohammadzadeh-aslReza YektaAhmad KeshtkarJafar Ezzati Nazhad DolatabadiAyuob AghanejadMiguel De La Guardiasubject
Cell Culture TechniquesQuantitative Structure-Activity RelationshipAntineoplastic Agents02 engineering and technologyMolecular Dynamics SimulationBiochemistry03 medical and health sciencesErlotinib HydrochlorideGefitinibStructural BiologymedicineHumansheterocyclic compoundsEpidermal growth factor receptorSurface plasmon resonanceReceptorneoplasmsMolecular BiologyProtein Kinase Inhibitors030304 developmental biology0303 health sciencesBinding SitesbiologyChemistryCell growthGeneral MedicineSurface Plasmon Resonance021001 nanoscience & nanotechnologySmall moleculerespiratory tract diseasesErbB ReceptorsMolecular Docking SimulationKineticsDocking (molecular)biology.proteinBiophysicsThermodynamicsErlotinib0210 nano-technologymedicine.drugProtein Bindingdescription
Abstract Epidermal growth factor receptor (EGFR) plays an important role in cell proliferation at non-small cell lung cancer (NSCLC). Therefore, targeted therapy of cancer via this kind of receptor is highly interested. Small molecule drugs such as erlotinib and gefitinib inhibit EGFR tyrosine kinase and thus suppress cell proliferation. At this paper, erlotinib interaction with EGFR on the cell surface was studied via surface plasmon resonance (SPR) and molecular docking methods. Kinetic parameters indicated that erlotinib affinity toward EGFR was increased through increment of temperature. The thermodynamic analysis showed that van der Waals and hydrogen binding forces play a major role in the interaction of erlotinib with EGFR. Docking results showed that Domain II in EGFR has role in the interaction with erlotinib. Besides, the binding energy for this interaction was −10.7 kcal/mol, which is suitable for binding of erlotinib to Domain II in EGFR.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2020-05-13 | International journal of biological macromolecules |