| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10798037 | Biochimica et Biophysica Acta (BBA) - Biomembranes | 2011 | 12 Pages |
Abstract
âºThe RW9 and R9 peptides are cell penetrating peptides but RL9 is not internalised. âºThe three peptides bind to the cell membrane. âºRW9 and R9 increase the fluidity of negatively charged lipid bilayers, RL9 does not. âºRW9 and R9 have ten fold more affinity for negatively charged liposomes than RL9. âºRL9 and RW9 become helical in presence of negatively charged liposomes.
Keywords
DMPGTOCSYDPCMLVCSDNOESYHSQCdMPCNOEITCMICPolyarginineDLSDSPGDSCdimyristoyl phosphatidylcholineSDSdimyristoyl phosphatidylglycerolCPPnuclear overhauser effectphosphatidic acidCholarge unilamellar vesicleChinese Hamster OvaryNMRCellular uptakeMinimal inhibitory concentrationdodecyl phosphocholinecircular dichroismsodium dodecyl sulfateNOE spectroscopyTotal correlation spectroscopyDiPoPEphosphatidylinositolphosphatidylcholinephosphatidylglycerolphosphatidylethanolaminePhosphatidylserinelactate dehydrogenaseLDHLUVHeteronuclear Single Quantum CorrelationHeparan sulfateDynamic Light Scatteringcell penetrating peptideCell-penetrating peptideAPAIsothermal titration calorimetryDifferential scanning calorimetryChondroitin sulfateCalorimetry
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Authors
Astrid Walrant, Isabelle Correia, Chen-Yu Jiao, Olivier Lequin, Eric H. Bent, Nicole Goasdoué, Claire Lacombe, Gérard Chassaing, Sandrine Sagan, Isabel D. Alves,