When the ionic strength of the buffer is reduced, the interaction is reversed. What is the difference between Reversed Phase (RP) HPLC and hydrophobic interaction chromatography (HIC)? Proteins with different degrees of surface hydrophobicity can be separated using hydrophobic interaction chromatography. The proteins are bound to the hydrophobic ligand on the HIC resin in a binding buffer with a high salt concentration. Reverse phase chromatography (RPC) refers to the highest resolution separation technique based on the hydrophobicity of the molecules in a mixture while hydrophobic interaction chromatography (HIC) refers to a type of separation technique based on the hydrophobicity but, operates under relatively mild conditions. Reversed-phase chromatography (RPC) is a liquid chromatography technique involving the separation of molecules on the basis of hydrophobic interactions between the solute molecules in the mobile phase and the ligands attached to the stationary phase. HIC and RPC are closely related techniques since both are based upon interactions between hydrophobic patches on the surface of biomolecules and the hydrophobic surfaces of a chromatography medium. From these observations two modes of protein chromatography have been developed, hydrophobic-interaction chromatography (HIC) and reversed-phase chromatography …

The hydrophobicity of RP-stationary phases is generally higher than that of HIC media. The variable hydrophobic nature of proteins allows their separation through differential hydrophobic surface interactions. In both cases, the stationary phase is more hydrophobic than the mobile phase.

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