The cell penetrating ability of the proapoptotic peptide, KLAKLAKKLAKLAK fused to the N-terminal protein transduction domain of translationally controlled tumor protein, MIIYRDLISH

Hyo Young Kim, Seunghoo Kim, Hyewon Youn, June Key Chung, Dong Hae Shin, Kyunglim Lee

Research output: Contribution to journalArticlepeer-review

46 Scopus citations

Abstract

We show here, that the proapoptotic peptide, KLAKLAKKLAKLAK (KLA), which by itself does not penetrate cell membranes, can do so when fused to a protein transduction domain derived from NH2-terminus of translationally controlled tumor protein (TCTP-PTD, MIIYRDLISH). Once inside the cell, the conjugated KLA exerts its proapoptotic activity to inhibit tumor growth. We evaluated the cellular uptake of KLA fused to TCTP-PTD (hereafter called TCTP-KLA) and its effect on cancer cell viability. The IC50 of TCTP-KLA was between 7 and 10 μmol/L. We also evaluated its anti-tumor activity in vivo by injecting it into xenografts of lung carcinoma in Balb/c nude mice. Tumor growth inhibition resulting from treatment with TCTP-KLA was better than that of TAT-KLA. These results suggest that TCTP-KLA can be applied to design cancer therapeutics.

Original languageEnglish
Pages (from-to)5262-5268
Number of pages7
JournalBiomaterials
Volume32
Issue number22
DOIs
StatePublished - Aug 2011

Keywords

  • Apoptosis
  • Cancer
  • Molecular imaging
  • Protein transduction domain
  • TCTP

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