A cyclic decapeptide, CQTPYYMNTC (1), which mimics the dimerization arm of the EGF receptor (EGFR), was previously found to be captured into cells. We have sought to investigate the promising potential of this peptide as an intracellular delivery vehicle directed to EGFR-positive cells. The selectivity of peptide 1 to the EGFR was confirmed by a positive correlation between the expression level of the receptor and the cellular uptake of peptide 1 as shown by siRNA knockdown of the EGFR. The proapoptotic domain (PAD) peptide ([KLAKLAK]2) has limited use due to a deficiency of cell membrane permeability resulting from cationic sequences and lack of specificity for cancer cells. As a proof-of-concept study, the cellular delivery of the PAD peptide was challenged by conjugation with peptide 1. The cellular uptake of a conjugated peptide 2, which was composed of peptide 1, the PAD peptide, and a linker cleavable with a protease, was evaluated by treatment of an EGFR-positive lung carcinoma cell line, A549. Significant suppression of proliferation by peptide 2 was shown in the results of a cell viability assay. The PAD peptide alone had no effect on the cells. The results suggest that peptide 1 is a promising lead compound as a new intracellular delivery vehicle for therapeutically effective peptides.