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Title: Fast membrane association is a crucial factor in the peptide Pep-1 translocation mechanism: a kinetic study followed by surface plasmon resonance
Author: Henriques, Sónia Troeira
Castanho, Miguel A. R. B.
Pattenden, Leonard Keith
Aguilar, Marie-Isabel
Keywords: Peptide–membrane interaction
Cell-penetrating peptides
Surface plasmon resonance
Membrane translocation
Cellular uptake
Peptide delivery
Issue Date: 2010
Publisher: Wiley-Blackwell
Citation: Peptide Science Volume 94 / Number 3 2010, 314–322
Abstract: The use of peptide carriers, termed ‘‘cell-penetrating peptides (CPPs)’’ has attracted much attention due to their potential for cellular delivery of hydrophilic molecules with pharmacological interest, overcoming the membrane barrier. These peptides are able to deliver attached cargos in a nontoxic manner, with the uptake mechanisms being either endosomally or physically driven. Pep-1 is a CPP of particular interest, not only due to outstanding delivery rates but also because its mechanism of membrane translocation is exclusively physically driven which appears to be dependent on a very high affinity for the phospholipid bilayer in the cell membrane. In this study, pep-1-lipid interactions were further explored by characterization of the pep-1-lipid association/dissociation by surface plasmon resonance. Although a high affinity of pep-1 for lipid bilayers was observed in all conditions tested, negatively charged phospholipids resulted in a larger peptide/lipid ratio. We also show that pep-1-membrane interaction is a fast process described by a multistep model initiated by peptide adsorption, primarily governed by electrostatic attractions, and followed by peptide insertion in the hydrophobic membrane core. In the context of a cellbased process, the translocation of pep-1 is a physical mechanism promoted by peptide primary amphipathicity and asymmetric properties of the membrane. This explains the high efficiency rates of pep-1 when compared with other CPPs.
Description: © 2010 Wiley Periodicals, Inc.
Peer review: yes
URI: hhtp://
ISSN: 0006-3525
Publisher Version: The definitive version is available at
Appears in Collections:IMM - Artigos em Revistas Internacionais

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