BIOT 158 |
| Monoclonal antibodies are gaining an increasing importance in diagnostic and therapeutic treatment of acute diseases such as cancer. However, the production and purification of these pharmaceuticals is still extremely expensive. Among the different methods for MAB purification, affinity chromatography is one of the most employed, despite its cost. In this work we present our computational investigation aimed at obtaining some guidelines for the rational design of affinity ligands, through the study of their interactions with both the antibody (IgG) and a model support material (agarose). This analysis was carried out performing MD simulations of the support-spacer-ligand-IgG system in explicit water. Two commercial ligands and several spacers, which differ for hydrophobicity and chemical structure, were considered. Binding energies were determined with the LIE and MM-PBSA approaches. The results were compared with experimental data and revealed that the interaction of the ligand with spacer and support can significantly affect the binding process. |
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Downstream Processing: Molecular Interactions and Modeling Approaches
3:00 PM-5:20 PM, Tuesday, August 21, 2007 BCEC -- 106, Oral
Division of Biochemical Technology |