Aggregation phenomena in CEX step were studied for a structurally unstable Fc-fusion protein.
Conformational changes in bound protein affect eluate aggregate level and aggregation reversibility.
Conditions that improve the structural integrity of bound protein help reduce aggregate formation.
CEX resin hydrophobicity contributes significantly to protein-resin interactions for partially unfolded protein.
An agarose resin immobilized with multi-functional ligands was prepared to verify the proposed hypothesis.