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Article Dans Une Revue Biochimica et Biophysica Acta - Molecular Cell Research Année : 2010

Secondary structure of cell-penetrating peptides controls membrane interaction and insertion.

Résumé

The clinical use of efficient therapeutic agents is often limited by the poor permeability of the biological membranes. In order to enhance their cell delivery, short amphipathic peptides called cell-penetrating peptides (CPPs) have been intensively developed for the last two decades. CPPs are based either on protein transduction domains, model peptide or chimeric constructs and have been used to deliver cargoes into cells through either covalent or non-covalent strategies. Although several parameters are simultaneously involved in their internalization mechanism, recent focuses on CPPs suggested that structural properties and interactions with membrane phospholipids could play a major role in the cellular uptake mechanism. In the present work, we report a comparative analysis of the structural plasticity of 10 well-known CPPs as well as their ability to interact with phospholipid membranes. We propose a new classification of CPPs based on their structural properties, affinity for phospholipids and internalization pathways already reported in the literature.
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Dates et versions

hal-00463228 , version 1 (17-03-2010)

Identifiants

Citer

Emelía Eiríksdóttir, Karidia Konate, Ulo Langel, Gilles Divita, Sébastien Deshayes. Secondary structure of cell-penetrating peptides controls membrane interaction and insertion.. Biochimica et Biophysica Acta - Molecular Cell Research, 2010, epub ahead of print. ⟨10.1016/j.bbamem.2010.03.005⟩. ⟨hal-00463228⟩
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