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Lipid vector for the delivery of peptides towards intracellular pharmacological targets
Author(s) -
GrasMasse Hélène
Publication year - 2003
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.631
Subject(s) - endosome , lipopeptide , intracellular , microbiology and biotechnology , endoplasmic reticulum , protease , context (archaeology) , peptide , biology , chemistry , biochemistry , enzyme , paleontology , genetics , bacteria
The ability of single‐chain lipopeptides to gain access to cellular compartments other than those related to degradation/recycling was first deduced from their capacity to deliver peptide antigens into MHC‐class I loading mechanisms. The ability of lipopeptides to escape complete endosome degradation was further illustrated by the selective inhibition of different protein kinase C isoenzymes and, more recently, the presentation of agonistic activity towards the interferon gamma receptor. Taken together, several independent results indicate that modification of a peptide by a single lipid chain confers upon it intracellular trafficking properties that can be used to deliver functional cargo peptides into living cells; the endoplasmic reticulum, cytosolic protease activity, sites of kinase activity, or even the signalling pathway associated with cytokine stimulation, all appear accessible to peptide modified by a single lipidic moiety. In this context, the interferon gamma receptor can be considered as a very discriminative pharmacological model, useful for the comparative evaluation of the cellular delivery of lipopeptides, as it allows the unambiguous tracking of their intact delivery into a wide range of cellular compartments. This model is now being used to probe the influence of the nature of the lipid moiety on the trafficking properties of lipopeptides. Copyright © 2003 John Wiley & Sons, Ltd.