One of the early biochemical changes of apoptotic cells is exposure of phosphatidylserine on the external surface of the plasma membrane. The aim of current study is targeting Phosphatidyl serine (PS) using radiolabeled LIKKPF, which was functionalized with HYNIC and aminooxy, radiolabeled with FDG and assessed in vitro and in vivo. Results showed LIKKPF has less affinity to PS compared to original phage peptide, but high enough for specific binding to apoptotic cells. It is concluded the low affinity of radiolabeled LIKKPF might be attributed to hydrophobicity of peptide, therefor peptides used in future studies should be more hydrophobic compared to LIKKPF.