Improving cell penetration of helical peptides stabilized by N-terminal crosslinked aspartic acids

Org Biomol Chem. 2017 Jan 4;15(2):459-464. doi: 10.1039/c6ob02501c.

Abstract

Cell penetration and nucleus translocation efficiency are important for the cellular activities of peptide therapeutics. For helical peptides stabilized by N-terminal crosslinked aspartic acid, correlations between their penetration efficiency/nucleus translocation and physicochemical properties were studied. An increase in hydrophobicity and isoelectric point will promote cellular uptake and nucleus translocation of stabilized helices.

MeSH terms

  • Aspartic Acid / chemistry*
  • Cell Survival / drug effects
  • Cell-Penetrating Peptides / chemical synthesis
  • Cell-Penetrating Peptides / chemistry*
  • Cell-Penetrating Peptides / pharmacology
  • Cross-Linking Reagents / chemistry*
  • Humans
  • Hydrophobic and Hydrophilic Interactions
  • MCF-7 Cells
  • Protein Stability

Substances

  • Cell-Penetrating Peptides
  • Cross-Linking Reagents
  • Aspartic Acid