Protein A affinity chromatography resins have for a long time been used to purify monoclonal antibodies (mAbs) by the bioprocess industry at all scales. The binding of protein A mainly takes place in the interphase between CH2 and CH3 in the Fc region of the mAb (constant domains 2 and 3 of the Ab heavy chains However, it is known that protein A also can bind to VH3 sequences located on the variable heavy chain of the Fab region.. Thus, this binding may also be utilized for the purification of target molecules derived from the variable domain of the heavy-chain antibodies of camelids, the so called VHHs.<br/><br/>When developing the high capacity, highly caustic tolerant protein A resin, MabSelect™ PrismA, the VH3 interaction was re-introduced during the maturation of the affinity ligand. Here we will show examples of purification of mAb derived fragments including Fab and VHH, focusing at binding characteristics e.g. binding capacities, elution conditions and purification performance. It will be demonstrated how the VHH can be purified directly from an <i>E. coli</i> harvest with good yield and at high load

Platform for purification of VHH-type antibody fragments

ACS Fall 2020 Virtual Meeting

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