Activation of cell-penetrating peptides by disulfide bridge formation of truncated precursors

Chem Commun (Camb). 2014 Jan 14;50(4):415-7. doi: 10.1039/c3cc46826g.

Abstract

A small library of oligoarginine peptides equipped with terminal cysteines was studied with respect to their cell-penetrating properties. The peptides themselves were inactive but gained the ability to enter cells upon extension of their sequence through disulfide bridge formation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell-Penetrating Peptides / chemistry*
  • Cell-Penetrating Peptides / metabolism
  • Disulfides / chemistry*
  • Flow Cytometry
  • Fluorescein-5-isothiocyanate / chemistry
  • HeLa Cells
  • Humans
  • Hydrogen-Ion Concentration
  • Microscopy, Confocal

Substances

  • Cell-Penetrating Peptides
  • Disulfides
  • Fluorescein-5-isothiocyanate