earticle

영어

Many of the known Cell penetrating pepetides (CPPs) share the common features of positively charged amino acids and amphipathicity. Unlike the other CPPs, PLAC was very short and possessed hydrophobic contents without basic amino acids. Translocation of PLAC across the cellular membrane was significantly affected by temperature, whereas ATP depletion and endocytosis inhibitors did not affect. And cellular uptake did not differ between D- and L-enantiomer of PLAC. PLAC was studied for its capacity to act as a vector molecules. The cargo protein, 120kDa β-galactosidase, was fused to the PLAC, results in translocation of the biologically active fusion protein to cytoplasm in cells. Furthermore, intraperitoneally injected PLAC fused β-galactosidase was almost delivered to each tissues in mice. More effective cell penetrating peptide (PLAC2W) was developed by amino acid substitutions of PLAC. Interestingly, uptake of PLAC-2W was inhibited by temperature, ATP depletion, and D-isomer unlike PLAC. Moreover, uptake of PLAC-2E significantly decreased by amiloride and slightly decreased by nystatin and filipin. These results indicate that cellular translocation of PLAC- 2W occur mainly through macropinocytosis pathway, while caveolae-mediated endocytosis is the minor pathway.