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The role of tryptophans on the cellular uptake and membrane interaction of arginine-rich cell penetrating peptides

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dc.relation.isnodouble60369b3d-f1c0-40d8-a097-bda630dcb808*
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hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorJOBIN, Marie-Lise
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorBLANCHET, Marine
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorHENRY, Sarah
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorCHAIGNEPAIN, Stephane
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorMANIGAND, Claude
hal.structure.identifierChimie biologique des membranes et ciblage thérapeutique [CBMCT - UMR 3666 / U1143]
dc.contributor.authorCASTANO, Sabine
dc.contributor.authorLECOMTE, S.
dc.contributor.authorBURLINA, F.
dc.contributor.authorSAGAN, S.
dc.contributor.authorD. ALVES, Isabel
dc.date.accessioned2020-09-03T08:02:07Z
dc.date.available2020-09-03T08:02:07Z
dc.date.issued2015
dc.identifier.issn0006-3002 (Print) 0006-3002
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/10971
dc.description.abstractEnCell-penetrating peptides (CPP) are able to efficiently transport cargos across cell membranes without being cytotoxic to cells, thus present a great potential in drug delivery and diagnosis. While the role of cationic residues in CPPs has been well studied, that of Trp is still not clear. Herein 7 peptide analogs of RW9 (RRWWRRWRR, an efficient CPP) were synthesized in which Trp were systematically replaced by Phe residues. Quantification of cellular uptake reveals that substitution of Trp by Phe strongly reduces the internalization of all peptides despite the fact that they strongly accumulate in the cell membrane. Cellular internalization and biophysical studies show that not only the number of Trp residues but also their positioning in the helix and the size of the hydrophobic face they form are important for their internalization efficacy, the highest uptake occurring for the analog with 3 Trp residues. Using CD and ATR-FTIR spectroscopy we observe that all peptides became structured in contact with lipids, mainly in alpha-helix. Intrinsic tryptophan fluorescence studies indicate that all peptides partition in the membrane in about the same manner (Kp~10(5)) and that they are located just below the lipid headgroups (~10A) with slightly different insertion depths for the different analogs. Plasmon Waveguide Resonance studies reveal a direct correlation between the number of Trp residues and the reversibility of the interaction following membrane washing. Thus a more interfacial location of the CPP renders the interaction with the membrane more adjustable and transitory enhancing its internalization ability.
dc.language.isoen
dc.title.enThe role of tryptophans on the cellular uptake and membrane interaction of arginine-rich cell penetrating peptides
dc.title.alternativeBiochimica et biophysica acta
dc.typeArticle de revue
dc.identifier.doi10.1016/j.bbamem.2014.11.013
dc.subject.halChimie/Matériaux
bordeaux.journalBiochim Biophys Acta
bordeaux.page593-602
bordeaux.volume1848
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248*
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN, UMR 5248)
bordeaux.issue2
bordeaux.institutionUniversité de Bordeaux
bordeaux.institutionBordeaux INP
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