Literature DB >> 17417137

[Transduction peptides: structural-functional analyses in model membranes].

Antonin Lamazière1, Gérard Chassaing, Germain Trugnan, Jesus Ayala-Sanmartin.   

Abstract

Peptide-membrane interaction is the first step required for peptide cell internalization. In this paper we studied the interactions of substance P, Penetratin and an amphiphilic 16mer (RL16) peptide in two different model membranes, giant unilamellar vesicles and large unilamellar vesicles. Penetratin was able to induce the formation of tubes inside the giant vesicles without changes in membrane permeability. On the contrary, RL16 induced the disruption of giant vesicles and the permeabilization of large vesicles. Substance P showed none of these effects.

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Year:  2006        PMID: 17417137     DOI: 10.1051/jbio:2006026

Source DB:  PubMed          Journal:  J Soc Biol        ISSN: 1295-0661


  3 in total

1.  Tubular structures in heterogeneous membranes induced by the cell penetrating peptide penetratin.

Authors:  Antonin Lamazière; Gérard Chassaing; Germain Trugnan; Jesus Ayala-Sanmartin
Journal:  Commun Integr Biol       Date:  2009-05

2.  Cholesterol re-organisation and lipid de-packing by arginine-rich cell penetrating peptides: Role in membrane translocation.

Authors:  Claudia Almeida; Ofelia Maniti; Margherita Di Pisa; Jean-Marie Swiecicki; Jesus Ayala-Sanmartin
Journal:  PLoS One       Date:  2019-01-23       Impact factor: 3.240

3.  The homeodomain derived peptide Penetratin induces curvature of fluid membrane domains.

Authors:  Antonin Lamazière; Claude Wolf; Olivier Lambert; Gérard Chassaing; Germain Trugnan; Jesus Ayala-Sanmartin
Journal:  PLoS One       Date:  2008-04-09       Impact factor: 3.240

  3 in total

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