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Title: The peptide carrier Pep-1 forms biologically efficient nanoparticle complexes

Abstract

Cell-penetrating peptides (CPPs) constitute a family of peptides whose unique characteristic is their ability to insert into and cross biological membranes. Cell-penetrating peptide carriers of the Pep family are amphipathic peptides which have been shown to deliver peptides and proteins into a wide variety of cells through formation of non-covalent complexes with their cargo. In this study, we have investigated the morphological features of different Pep-1/cargo complexes by scanning electron microscopy and light scattering measurements. We provide first-time evidence that biologically efficient complexes of Pep-1/p27Kip tumour suppressor physically exist in the form of discrete nanoparticles. Moreover, we have characterized the relationship between the Pep-1/cargo ratio, the size and homogeneity of the nanoparticles formed, and their efficiency in delivering the cargo into cells, and report that particle size and homogeneity is both directly dependent on the ratio of Pep-1/cargo formulations, and responsible for their biological efficiency.

Authors:
 [1];  [2];  [3];  [2]
  1. Centro Nacional de Investigaciones Metalurgicas-CSIC, Avda Gregorio del Amo 8, 28040 Madrid (Spain)
  2. Centre de Recherches en Biochimie Macromoleculaire, CNRS-FRE2593, 1919 Route de Mende, 34293 Montpellier (France)
  3. Centre de Recherches en Biochimie Macromoleculaire, CNRS-FRE2593, 1919 Route de Mende, 34293 Montpellier (France). E-mail: gilles.divita@crbm.cnrs.fr
Publication Date:
OSTI Identifier:
20979880
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 355; Journal Issue: 4; Other Information: DOI: 10.1016/j.bbrc.2007.02.046; PII: S0006-291X(07)00295-1; Copyright (c) 2007 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; CALVES; CARGO; CARRIERS; COMPLEXES; FLUORESCENCE; LIGHT SCATTERING; MORPHOLOGY; NANOSTRUCTURES; PARTICLE SIZE; PEPTIDES; PHOSPHOENOLPYRUVATE; SCANNING ELECTRON MICROSCOPY

Citation Formats

Munoz-Morris, Maria A., Heitz, Frederic, Divita, Gilles, and Morris, May C.. The peptide carrier Pep-1 forms biologically efficient nanoparticle complexes. United States: N. p., 2007. Web. doi:10.1016/j.bbrc.2007.02.046.
Munoz-Morris, Maria A., Heitz, Frederic, Divita, Gilles, & Morris, May C.. The peptide carrier Pep-1 forms biologically efficient nanoparticle complexes. United States. doi:10.1016/j.bbrc.2007.02.046.
Munoz-Morris, Maria A., Heitz, Frederic, Divita, Gilles, and Morris, May C.. Fri . "The peptide carrier Pep-1 forms biologically efficient nanoparticle complexes". United States. doi:10.1016/j.bbrc.2007.02.046.
@article{osti_20979880,
title = {The peptide carrier Pep-1 forms biologically efficient nanoparticle complexes},
author = {Munoz-Morris, Maria A. and Heitz, Frederic and Divita, Gilles and Morris, May C.},
abstractNote = {Cell-penetrating peptides (CPPs) constitute a family of peptides whose unique characteristic is their ability to insert into and cross biological membranes. Cell-penetrating peptide carriers of the Pep family are amphipathic peptides which have been shown to deliver peptides and proteins into a wide variety of cells through formation of non-covalent complexes with their cargo. In this study, we have investigated the morphological features of different Pep-1/cargo complexes by scanning electron microscopy and light scattering measurements. We provide first-time evidence that biologically efficient complexes of Pep-1/p27Kip tumour suppressor physically exist in the form of discrete nanoparticles. Moreover, we have characterized the relationship between the Pep-1/cargo ratio, the size and homogeneity of the nanoparticles formed, and their efficiency in delivering the cargo into cells, and report that particle size and homogeneity is both directly dependent on the ratio of Pep-1/cargo formulations, and responsible for their biological efficiency.},
doi = {10.1016/j.bbrc.2007.02.046},
journal = {Biochemical and Biophysical Research Communications},
number = 4,
volume = 355,
place = {United States},
year = {Fri Apr 20 00:00:00 EDT 2007},
month = {Fri Apr 20 00:00:00 EDT 2007}
}