Comparison of the interaction, positioning, structure induction and membrane perturbation of cell-penetrating peptides and non-translocating variants with phospholipid vesicles

Mazin Magzoub, L. E.Göran Eriksson, Astrid Gräslund

Research output: Contribution to journalArticle

Abstract

Cell-penetrating peptides (CPPs) are able to translocate and carry cargo molecules across cell membranes. Using fluorescence techniques (polarization and quenching) and CD spectroscopy we studied the interaction, conformation and topology of two such peptides, transportan and 'penetratin' (pAntp), and two variants of differing translocating abilities, with small phospholipid vesicles of varying charge density. The induced structure of transportan is always helical independent of vesicle surface charge. pAntp and its two variants interact significantly only with negatively charged vesicles. The induced secondary structure depends on membrane charge and lipid/peptide ratio. The degree of membrane perturbation, evidenced by fluorescence polarization, of pAntp and its variants is related to their secondary structure. In the helical state, the peptides have little effect on the membrane. Under conditions where pAntp and its variants are converted into β-structures, they cause membrane perturbation. Oriented CD suggests that the two CPPs (pAntp and transportan) in their helical state lie along the vesicle surface, while the two pAntp variants appear to penetrate deeper into the membrane.

Original languageEnglish (US)
Pages (from-to)271-288
Number of pages18
JournalBiophysical Chemistry
Volume103
Issue number3
DOIs
StatePublished - Mar 25 2003

Keywords

  • Antennapedia
  • Penetratin
  • Phospholipid vesicles
  • Structure induction
  • Translocation
  • Transportan

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Organic Chemistry

Fingerprint Dive into the research topics of 'Comparison of the interaction, positioning, structure induction and membrane perturbation of cell-penetrating peptides and non-translocating variants with phospholipid vesicles'. Together they form a unique fingerprint.

  • Cite this