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Ionpair-pi interactions favor cell penetration of arginine/tryptophan-rich cell-penetrating peptides

dc.rights.licenseopenen_US
dc.contributor.authorWALRANT, Astrid
dc.contributor.authorBAUZA, Antonio
dc.contributor.authorGIRARDET, Claudia
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorALVES, Isabel
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorLECOMTE, Sophie
dc.contributor.authorILLIEN, Francoise
dc.contributor.authorCARDON, Sebastien
dc.contributor.authorCHAIANANTAKUL, Natpasit
dc.contributor.authorPALLERLA, Manjula
dc.contributor.authorBURLINA, Fabienne
dc.contributor.authorFRONTERA, Antonio
dc.contributor.authorSAGAN, Sandrine
dc.date.accessioned2020-04-22T09:33:23Z
dc.date.available2020-04-22T09:33:23Z
dc.date.issued2020
dc.identifier.issn0005-2736en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/4333
dc.description.abstractEnCell-penetrating peptides (CPPs) internalization occurs both by endocytosis and direct translocation through the cell membrane. These different entry routes suggest that molecular partners at the plasma membrane, phospholipids or glycosaminoglycans (GAGs), bind CPPs with different affinity or selectivity. The analysis of sequence-dependent interactions of CPPs with lipids and GAGs should lead to a better understanding of the molecular mechanisms underlying their internalization. CPPs are short sequences generally containing a high number of basic arginines and lysines and sometimes aromatic residues, in particular tryptophans. Tryptophans are crucial residues in membrane-active peptides, because they are important for membrane interaction. Membrane-active peptides often present facial amphiphilicity, which also promote the interaction with lipid bilayers. To study the role of Trp and facial amphiphilicity in cell interaction and penetration of CPPs, a nonapeptide series containing only Arg, Trp or D-Trp residues at different positions was designed. Our quantitative study indicates that to maintain/increase the uptake efficiency, Arg can be advantageously replaced by Trp in the nonapeptides. The presence of Trp in oligoarginines increases the uptake in cells expressing GAGs at their surface, while it compensates for the loss of charge interactions from Arg and maintains similar peptide uptake in GAG-deficient cells. In addition, we show that facial amphiphilicity is not required for efficient uptake of these nonapeptides. Thermodynamic analyses point towards a key role of Trp that highly contributes to the binding enthalpy of complexes formation. Density functional theory (DFT) analysis highlights that salt bridge-pi interactions play a crucial role for the GAG-dependent entry mechanisms.
dc.language.isoENen_US
dc.subject.enCell-penetrating-peptide
dc.subject.enIonpair-pi interaction
dc.subject.enGlycosaminoglycan
dc.subject.enLipid membrane
dc.subject.enTryptophan
dc.subject.enArginine
dc.title.enIonpair-pi interactions favor cell penetration of arginine/tryptophan-rich cell-penetrating peptides
dc.typeArticle de revueen_US
dc.identifier.doi10.1016/j.bbamem.2019.183098
dc.subject.halChimie/Matériauxen_US
bordeaux.journalBiochimica et biophysica acta. Biomembranesen_US
bordeaux.page183098-183098en_US
bordeaux.volume1862en_US
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248en_US
bordeaux.issue2en_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
hal.identifierhal-02959877
hal.version1
hal.date.transferred2020-10-07T09:08:33Z
hal.exporttrue
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