The J-domain of heat shock protein 40 can enhance the transduction efficiency of arginine-rich cell-penetrating peptides

Biomed Res Int. 2015:2015:698067. doi: 10.1155/2015/698067. Epub 2015 May 17.

Abstract

Sense and antisense oligonucleotide pairs encoding cell-penetrating peptides PTD (Tat47-57), DPV3A, E162, pVEC, R11, and TP13 were used to construct two sets of pET22b-CPP-DsRed and pET22b-CPP-J-DsRed vectors for CPP-DsRed and CPP-J-DsRed recombinant proteins expression. PTD-DsRed, DPV3A-DsRed, PTD-J-DsRed, and DPV3A-J-DsRed recombinant proteins were expressed in a soluble form. PTD-J-DsRed and DPV3A-J-DsRed recombinant proteins were able to escape from E. coli host cells into the culture medium. The membrane-penetrating activity of PTD-J-DsRed and DPV3A-J-DsRed recombinant proteins to mammalian cells was more effective than that of PTD-DsRed and DPV3A-DsRed. The route of the cellular membrane translocation of these recombinant proteins is suggested via macropinocytosis followed by an endosomal escape pathway.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Line, Tumor
  • Cell-Penetrating Peptides* / chemistry
  • Cell-Penetrating Peptides* / pharmacology
  • HSP40 Heat-Shock Proteins* / chemistry
  • HSP40 Heat-Shock Proteins* / pharmacology
  • Humans
  • Protein Structure, Tertiary
  • Transduction, Genetic / methods*

Substances

  • Cell-Penetrating Peptides
  • HSP40 Heat-Shock Proteins