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Article Dans Une Revue Biochimica et Biophysica Acta:Biomembranes Année : 2006

A non-covalent peptide-based strategy for protein and peptide nucleic acid transduction

Résumé

The development of therapeutic peptides and proteins is limited by the poor permeability and the selectivity of the cell membrane. The discovery of protein transduction domains has given a new hope for administration of large proteins and peptides in vivo. We have developed a non-covalent strategy for protein transduction based on an amphipathic peptide, Pep-1, that consists of a hydrophobic domain and a hydrophilic lysine-rich domain. Pep-1 efficiently delivers a variety of fully biologically active peptides and proteins into cells, without the need for prior chemical cross-linking or chemical modifications. The mechanism through which Pep-1 delivers active macromolecules does not involve the endosomal pathway and the dissociation of the Pep-1/macromolecule particle occurs immediately after it crosses the cell membrane. Pep-1 has been successfully applied to the screening of therapeutic peptides in vivo and presents several advantages: stability in physiological buffer, lack of toxicity and of sensitivity to serum. In conclusion, Pep-1 technology could contribute significantly to the development of fundamental and therapeutic applications and be an alternative to covalent protein transduction domain-based technologies.

Dates et versions

hal-03116867 , version 1 (20-01-2021)

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Edwige Gros, Sébastien Deshayes, May Morris, Gudrun Aldrian-Herrada, Julien Depollier, et al.. A non-covalent peptide-based strategy for protein and peptide nucleic acid transduction. Biochimica et Biophysica Acta:Biomembranes, 2006, 1758 (3), pp.384-393. ⟨10.1016/j.bbamem.2006.02.006⟩. ⟨hal-03116867⟩
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