Self-assembling mini cell-penetrating peptides enter by both direct translocation and glycosaminoglycan-dependent endocytosis

Saskia A Bode; Marion Thévenin; Chérine Bechara; Sandrine Sagan; Sarah Bregant; Solange Lavielle; Gérard Chassaing; Fabienne Burlina

doi:10.1039/c2cc33240j

Self-assembling mini cell-penetrating peptides enter by both direct translocation and glycosaminoglycan-dependent endocytosis

Chem Commun (Camb). 2012 Jul 21;48(57):7179-81. doi: 10.1039/c2cc33240j. Epub 2012 Jun 13.

Authors

Saskia A Bode¹, Marion Thévenin, Chérine Bechara, Sandrine Sagan, Sarah Bregant, Solange Lavielle, Gérard Chassaing, Fabienne Burlina

Affiliation

¹ UPMC Univ Paris 06, UMR 7203, LBM, F-75005, Paris, France.

PMID: 22692031
DOI: 10.1039/c2cc33240j

Abstract

A small library of cell-penetrating peptides (CPPs) containing a minimized cationic domain and a lipophilic domain of different size was studied. CPPs that could self-assemble were found to enter cells more efficiently, triggering a glycosaminoglycan-dependent pathway.

MeSH terms

Amino Acid Sequence
Animals
CHO Cells
Cell Membrane Permeability
Cell-Penetrating Peptides / chemistry*
Cell-Penetrating Peptides / metabolism*
Cricetinae
Endocytosis
Glycosaminoglycans / metabolism*
Molecular Sequence Data
Peptide Library
Protein Kinase Inhibitors / administration & dosage*

Substances

Cell-Penetrating Peptides
Glycosaminoglycans
Peptide Library
Protein Kinase Inhibitors