What is Hydrophobic interaction chromatography?
Hydrophobic interaction chromatography (HIC) is a liquid chromatography technique that separates biomolecules according to hydrophobicity. Although most hydrophobic amino acids are buried in the interior of globular proteins, some of them are exposed on the protein surface. These can interact with hydrophobic ligands on the HIC gel. The amount of exposed hydrophobic amino acids differs between proteins and so does the ability of proteins to interact with HIC gels. HIC is complementary to ion exchange (IEX) and gel filtration (GF) and high overall resolutions are obtained when HIC is combined with other LC techniques. Since HIC is an adsorptive technique, gradient or step elution can be applied and the sample elutes in concentrated form. High salt concentrations are needed to adsorb the sample to the HIC gel. This makes it especially well-suited as a capture step after ammonium sulfate precipitation and as a next step after IEX, since no or very simple inter-step conditioning will be ne
