A hybrid biomimetic ligand composed of three amino acid residues and a hydrophobic charge-induction group was developed and its performance of immunoglobulin G (IgG) purification from human serum was evaluated. The sequence of peptides of the hybrid ligand (Phenylalanine-Tyrosine-Glutamate-"5-amino-benzimidazole", FYE-ABI) was designed and evaluated via molecular simulation, and the ligand was synthesized and coupled onto agarose beads. Adsorption isotherm results showed that the optimum IgG adsorption was found at pH 7.0 with saturated adsorption capacity of 91 mg/mL resin and dissociation constant of 1.6 mu M. The hybrid biomimetic resin showed high separation purity of 99.0% and recovery of 91.5% when used in IgG separation from human serum albumin (HSA) containing solutions. Moreover, study on IgG separation from human serum showed that the hybrid biomimetic ligand could provide comparable IgG purity (93.9%) and recovery (88.9%), but much milder elution condition (pH 4.5) as those of Protein A affinity chromatography. The combination of biomimetic and hydrophobic charge-induction chromatography presented high selectivity and mild elution for antibody purification.