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A step‐wise approach to define binding mechanisms of surrogate viral particles to multi‐modal anion exchange resin in a single solute system

Abstract

Multi‐modal anion exchange resins combine properties of both anion exchange and hydrophobic interaction chromatography for commercial protein polishing and may provide some viral clearance as well. From a regulatory viral clearance claim standpoint, it is unclear if multi‐modal resins are truly orthogonal to either single‐mode anion exchange or hydrophobic interaction columns. To answer this, a strategy of solute surface assays and High Throughput Screening of resin in concert with a scale‐down model of large scale chromatography purification was employed to determine the predominant binding mechanisms of a panel of bacteriophage (i.e. PR772, PP7, and ΦX174) to multi‐modal and single mode resins under various buffer conditions. The buffer conditions were restricted to buffer environments suggested by the manufacturer for the multi‐modal resin. Each phage was examined for estimated net charge expression and relative hydrophobicity using chromatographic based methods. Overall, PP7 and PR772 bound to the multimodal resin via both anionic and hydrophobic moieties, while ΦX174 bound predominantly by the anionic moiety. This article is protected by copyright. All rights reserved

Authors:   Matthew Brown, Sarah Johnson, Kurt Brorson, Scott Lute, David Roush
Journal:   Biotechnology and Bioengineering
Year:   2017
Pages:   n/a
DOI:   10.1002/bit.26251
Publication date:   21-Jan-2017
Facts, background information, dossiers
  • Exchange
  • Single
  • resins
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