A new peptide motif present in the protective antigen of anthrax toxin exerts its efficiency on the cellular uptake of liposomes and applications for a dual-ligand system

Int J Pharm. 2011 Jun 30;412(1-2):106-14. doi: 10.1016/j.ijpharm.2011.03.010. Epub 2011 Mar 15.

Abstract

Protective antigen (PA) is a nontoxic protein present in anthrax toxin. Domain 4 of PA (PA-D4) acts as a receptor binding site for tumor endothelial marker 8 (TEM8). In this study, KYND motif from PA-D4 was utilized as a ligand against TEM8. The efficiency of KYND motif on cellular association was assessed by evaluating the cellular uptake of PEGylated liposomes (PEG-LPs) in TEM8 positive and negative cells. The peptide was attached on the top of the PEG of PEG-LP. Compared to PEG-LP, KYND modified PEG-LP (KYND-PEG-LP) enhanced the cellular uptake to a greater extent in all cell lines. Based on the inhibition assay, no receptor involvement was observed in the cellular association of KYND-PEG-LP, suggesting that KYND motif functions as a cell penetrating peptide (CPP) which facilitated the internalization of PEG-LP via clathrin mediated endocytosis pathway. Further enhancement of cellular uptake was observed when KYND-PEG-LP was combined with octaarginine (R8) on the surface of lipid membrane as dual-CPP ligand formulation, however, when PEG-LP combined with only R8, only negligible enhancement was observed. These findings suggest that two CPP ligands act in a synergistic fashion; therefore the dual-CPP ligand based liposomal formulation can be assumed to be an effective delivery system.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Animals
  • Antigens, Bacterial / chemistry*
  • Bacterial Toxins / chemistry*
  • Binding, Competitive
  • Biological Transport
  • Biomarkers, Tumor / metabolism
  • Cell Line
  • Cell-Penetrating Peptides / chemistry
  • Cell-Penetrating Peptides / metabolism*
  • Cells, Cultured
  • Drug Carriers / metabolism*
  • Drug Delivery Systems / methods
  • HeLa Cells
  • Humans
  • Ligands
  • Liposomes
  • Mice
  • Microfilament Proteins
  • Neoplasm Proteins / metabolism
  • Oligopeptides / chemistry
  • Oligopeptides / metabolism*
  • Peptide Fragments / chemistry
  • Peptide Fragments / metabolism*
  • Phosphatidylethanolamines / chemistry
  • Phosphatidylethanolamines / metabolism
  • Polyethylene Glycols / chemistry
  • Polyethylene Glycols / metabolism
  • Receptors, Cell Surface / metabolism
  • Receptors, Peptide / metabolism

Substances

  • ANTXR1 protein, human
  • Antigens, Bacterial
  • Antxr1 protein, mouse
  • Bacterial Toxins
  • Biomarkers, Tumor
  • Cell-Penetrating Peptides
  • Drug Carriers
  • Ligands
  • Liposomes
  • Microfilament Proteins
  • Neoplasm Proteins
  • Oligopeptides
  • Peptide Fragments
  • Phosphatidylethanolamines
  • Receptors, Cell Surface
  • Receptors, Peptide
  • anthrax toxin
  • octaarginine
  • 1,2-distearoylphosphatidylethanolamine
  • Polyethylene Glycols