Anion exchange and hydrophobic interaction chromatography are very common in commercial downstream bioprocessing. Multimodal anion exchange resin combines both ionic and hydrophobic properties to clear product impurities as well as possibly providing viral clearance. In regulatory submissions, orthogonal viral clearance steps are claimed and added together for a net process viral clearance. An interesting issue arises when considering if multimodal resins can be considered orthogonal to other chromatography steps in a process that contains purely anion exchange and/or hydrophobic interaction unit operations.<br/>In this project we attempted to define the interaction between the viruses and the resin surface in order to provide clarity on how to justify orthogonal viral clearance. Utilizing High Throughput Screening, the multimodal resin and its individual functional groups were tested to their failure limit by manipulating viral titer and buffer conditions of the load. In concert with solute surface assays, individual electrostatic and hydrophobic contributions were dissected for a commonly employed multimodal resin. Select batch conditions were then scaled up to column testing to determine if the same mechanistic binding trends from batch experiments could be transferred to a dynamic system.<br/>

Leveraging solute surface analytics and high throughput screening to define binding mechanisms of virus particles to multimodal anion exchange resin

251st National Meeting (2016)

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