Purification of peptides typically includes costly reverse phase processes which utilize high pressure and large volumes of solvent. For two conjugated peptides, chromatography process development targeted a low pressure aqueous process that could achieve target product purities of ≥95%, comparable to purities seen with traditional reverse phase. A high throughput screening approach of different modalities was used to identify binding and elution conditions on a cation exchange resin and small scale columns were used in order to assess impurity removal and process yield. The parameters for load and gradient elution were optimized to increase product purity and process productivity with a wide operating window identified where high purity and productivity are achieved.<br/>Computational modeling was then used to validate experimental chromatography results and to gain insight on the effect of the chemical modifications on the surface properties of the two peptides. Both modelling and experimental data showed that with optimization, reverse phase can be replaced by cation exchange to achieve similar purities for conjugated peptides with double the productivity.

Cation exchange as a single purification step alternative to reverse phase for conjugated peptides

2019 Spring National Meeting

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