title: Activation of cell-penetrating peptides by disulfide bridge formation of truncated precursors.
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.
authors.affiliation: Radboud University Nijmegen, Institute for Molecules and Materials, Bio-organic chemistry, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands. d.lowik@science.ru.nl.
authors.forename: Saskia A
authors.initials: SA
authors.lastname: Bode
authors.forename: Rike
authors.initials: R
authors.lastname: Wallbrecher
authors.forename: Roland
authors.initials: R
authors.lastname: Brock
authors.forename: Jan C M
authors.initials: JC
authors.lastname: van Hest
authors.forename: Dennis W P M
authors.initials: DW
authors.lastname: Löwik
mesh_terms: D057846:Cell-Penetrating Peptides / Q000737:chemistry* / Q000378:metabolism; D004220:Disulfides / Q000737:chemistry*; D005434:Flow Cytometry; D016650:Fluorescein-5-isothiocyanate / Q000737:chemistry; D006367:HeLa Cells; D006801:Humans; D006863:Hydrogen-Ion Concentration; D018613:Microscopy, Confocal
chemical_list: D057846:Cell-Penetrating Peptides; D004220:Disulfides; D016650:Fluorescein-5-isothiocyanate