Ion-exchange chromatography is used in biopharmaceutical downstream processes to reduce product-related impurity levels. Because protein aggregate levels can be considered as a critical quality attribute, the removal of aggregated protein species is of primary importance. The addition of polyethylene glycol (PEG) to the mobile phase in ion-exchange chromatography was found to significantly improve the chromatographic separation of monomers from aggregates. In this work, linear gradient elution experiments with monomeric and aggregated samples of a monoclonal antibody were performed on a strong cation exchange resin at different PEG concentrations to investigate the underlying effects responsible for the observed selectivity improvement. PEG is well known to be excluded from a surface layer volume around the protein and the stationary phase; thus, enhancing adsorption of the preferentially hydrated protein to the hydrated stationary phase. The exclusion volume depends on the accessible surface area of the protein leading to a stronger influence of PEG on larger protein species and thus an improved separation of monomer and aggregates. This hypothesis could be consolidated comparing the distribution equilibrium in PEG solution to that in water by calculating equilibrium constants and transfer free energies using the chromatographic data from the linear gradient elution experiments performed at different pH values.