A polypeptide with 26 amino acid residues was designed and synthesized. Its N terminal was composed of multiple lysine residues, which played as a DNA condensing agent, whereas the C terminal was the receptor binding domain of bFGF (Tyr114-Tyr123 ). Through a spontaneous self-assembly process with electrostatic interaction, the synthetic peptide combined with a luciferase expression vector, pEBluc, to mediate internalization of peptide-nucleic acid complex via bFGF receptors. Significant luciferase activity was detected 48 hours after adding this complex directly to the culture medium of endot...
