Alternative antibody-binding affinity ligands are expected to support robust time- and cost-effective antibody purification with rapid improvement of upstream productivity and demand on downstream process optimization. Five new tetrapeptide biomimetic affinity ligands (FYRH, HWRH, YHRI, HYRF, and FHRA) were screened by modeling the molecular interaction mechanism between tetrapeptide ligands and the Fc fragment of IgG with molecular dynamics simulation and the flexible docking method, and the corresponding five resins were prepared in this work to evaluate their adsorption characteristics of human immunoglobulin G (hIgG). The results showed that the binding capacities to hIgG of the five resins showed a strong pH-dependency, which was high at pH 7.0-9.0, and extremely low at pH 5.0-6.0, providing a benefit choice to separate hIgG. The dynamic binding capacities (DBC) at 10% breakthrough of five resins could reach up to 28-37 mg/mL(gel), and Ac-FYRH-4FF resin showed the best adsorption performance. The elution test results with Ac-FYRH-4FF resin indicated that hIgG could be eluted mildly at pH 5.0 with a 96.5% recovery, meaning that this resin can be considered as a powerful candidate of alternative biomimetic affinity chromatographic resin.