Phage display is a technology which can display the foreign peptides on the surface of the phages interacting with exterior molecules/materials. Such kind of peptides could demonstrate the same recognition and interaction capability compared to their native antibody molecules and yet possessing reduced sensitivity and improved stability characteristics. Phage display technique has been used to screen and identify the antibody mimicking peptides. In our study, the 'biopanning' was carried out by incubating a library of phage-displayed 12-mer peptides sequence (ca. 109 clones expressed as fusions on M13 pIII protein) on a solid surface coated with the target antigen (human IgG), washing away the unbound phages, and eluting the specifically bound phages. The eluted phages were taken through additional binding cycles to enrich the pool in favor of binding sequences. Our preliminary experiments resulted in 4 clones (F9, D1, G5, A10) showing specific binding to human IgG through enzyme linked immunosorbent assay (ELISA). Among them, F9 showed the highest affinity (Kd = 6.2 nM), only one order of magnitude lower than the native anti-human IgG (0.66 nM). Four 12-mer peptides having the specific amino acid sequences of the selected phages were chemically synthesized. Binding affinities of the synthesized peptides to hIgG were monitored using Surface Plasmon Resonance (SPR). The peptide D1 had a higher binding affinity against hIgG than the rest. This peptide was attached onto streptavidin -coated magnetic bead to determine the hIgG capturing ability and later to compare with immobilized anti- hIgG-bead. The result suggested that identified mimicking peptide from phage display was capable of capturing hIgG and showed the potential for immuno-magnetic separation.