期刊
JOURNAL OF PEPTIDE SCIENCE
卷 14, 期 4, 页码 482-487出版社
WILEY
DOI: 10.1002/psc.1003
关键词
cell-penetrating peptides; peptide-membrane interactions; translocation mechanism; drug delivery; anti-microbial peptides
The Cell membrane is impermeable for most peptides, proteins, and oligonucleotides. Moreover, some cationic peptides, the so-called cell-penetrating peptides (CPPs), are able to translocate across the membrane. This observation has attracted much attention because these peptides can be covalently coupled to different macromolecules, which are efficiently delivered inside the cell. The mechanism used by these peptides to pass across the membrane is a controversial matter of debate. It has been suggested that endocytosis is the main mechanism of internalization and this was confirmed by several studies for different peptides. Pep-1 is an exception worthy of attention for its ability to translocate cargo macromolecules without the need to be covalently attached to them. A preferential internalization by an endocytosis-independent mechanism was demonstrated both in vitro and in vivo. Pep-1 has a high affinity to lipidic membranes, it is able to insert and induce local destabilization in the lipidic bilayer, although without pore formation. No cytotoxic effects were found for pep-1 concentrations where translocation is fully operative. At much higher concentrations, membrane disintegration takes place by a detergent-like mechanism that resembles anti-microbial peptide activity. In this review, the ability of pep-1 to transverse the membrane by an endocytosis-independent mechanism, not mediated by pores as well as an ability to induce membrane disintegration at high peptide concentration, is demonstrated. Copyright (c) 2008 European Peptide Society and John Wiley & Sons, Ltd.
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