| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10797488 | Biochimica et Biophysica Acta (BBA) - Biomembranes | 2012 | 10 Pages |
Abstract
⺠Internalization of a cargo by glycosylated CPPs was investigated by MALDI-TOF MS. ⺠Substitution of tryptophan(s) in the CPP decreased the internalization efficiency. ⺠The behavior of these CPPs was studied with model membranes. ⺠The insertion of CPPs is enthalpy driven and is related to the number of tryptophan. ⺠These CPPs have a certain propensity to aggregate in contact with the lipid surface.
Keywords
TISGAGdMPCRP-HPLCTFADSCITCdimyristoylphosphatidylcholineNMPN-MethylpyrrolidoneDMPGDSPGMALDI-TOFTriisopropylsilaneCPPLUVsDMEMMLVsDMFDulbecco's modified Eagle's mediummultilamellar vesiclesTrifluoroacetic acidCholarge unilamellar vesiclesChinese Hamster OvaryTryptophanInternalizationRoom temperaturediisopropylethylaminedimethylformamidematrix-assisted laser desorption ionization time-of-flightATR spectroscopyAttenuated total reflection spectroscopyMass spectrometryMicrocalorimetryDIPEAcell penetrating peptideCell-penetrating peptideIsothermal titration calorimetryDifferential scanning calorimetryGlycosaminoglycanGlycosylation
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Authors
Pascaline Lécorché, Astrid Walrant, Fabienne Burlina, Laurence Dutot, Sandrine Sagan, Jean-Maurice Mallet, Bernard Desbat, Gérard Chassaing, Isabel D. Alves, Solange Lavielle,