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            <title xml:lang="en">The peptide carrier Pep-1 forms biologically efficient nanoparticle complexes</title>
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                <forename type="first">Maria</forename>
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                <title xml:lang="en">The peptide carrier Pep-1 forms biologically efficient nanoparticle complexes</title>
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                    <forename type="first">Maria</forename>
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                <term xml:lang="en">Morphology</term>
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                <term xml:lang="en">Peptide and protein delivery</term>
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              <p>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</p>
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