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Cell penetrating peptides (CPPs) with intrinsic biological activities offer a novel strategy for the modulation of intracellular events. QSAR analysis identified CPPs within human cytochrome c. Two such sequences, Cyt c(77-101) and Cyt c(86-101), induced tumor cell apoptosis, thus mimicking the role of Cyt c as a key regulator of programmed cell death. Quantitative analyses confirmed that Cyt c(77-101) is an extremely efficient CPP. Thus, Cyt c(77-101) was selected for modification to incorporate target-specific peptidyl motifs. Chimeric N-terminal extension with a target mimetic of FG nucleoporins significantly enhanced the apoptogenic potency of Cyt c(77-101) to a concentration readily achievable in vivo. Moreover, this construct, Nup153-Cyt c, facilitates the dramatic redistribution of nuclear pore complex proteins and thus propounds the nuclear pore complex as a novel target for the therapeutic induction of apoptosis.

Original publication




Journal article


Chem Biol

Publication Date





735 - 744


Algorithms, Amino Acid Motifs, Amino Acid Sequence, Animals, Apoptosis, Biomimetic Materials, Cell Line, Tumor, Cell Nucleus, Cytochromes c, Drug Design, Humans, Models, Molecular, Molecular Sequence Data, Peptide Fragments, Protein Structure, Secondary, Protein Transport