Fast membrane association is a crucial factor in the peptide pep-1 translocation mechanism: A kinetic study followed by surface plasmon resonance

摘要: The use of peptide carriers, termed "cell-penetrating peptides (CPPs)" has attracted much attention due to their potential for cellular delivery hydrophilic molecules with pharmacological interest, overcoming the membrane barrier. These are able deliver attached cargos in a nontoxic manner, uptake mechanisms being either endosomally or physically driven. Pep-1 is CPP particular not only outstanding rates but also because its mechanism translocation exclusively driven which appears be dependent on very high affinity phospholipid bilayer cell membrane. In this study, pep-1-lipid interactions were further explored by characterization association/dissociation surface plasmon resonance. Although pep-1 lipid bilayers was observed all conditions tested, negatively charged phospholipids resulted larger peptide/lipid ratio. We show that pep-1-membrane interaction fast process described multistep model initiated adsorption, primarily governed electrostatic attractions, and followed insertion hydrophobic core. context cell-based process, physical promoted primary amphipathicity asymmetric properties This explains efficiency when compared other CPPs.