Please use this identifier to cite or link to this item:
|Title:||S4(13)-PV cell-penetrating peptide induces physical and morphological changes in membrane-mimetic lipid systems and cell membranes: Implications for cell internalization||Authors:||Cardoso, Ana M. S.
Cardoso, Ana L.
Morais, Catarina M.
Lima, Maria C. Pedroso de
Jurado, Amália S.
|Keywords:||Cell-penetrating peptide; Membrane model; DSC; Fluorescence polarization; WAXS/SAXS; Electron microscopy||Issue Date:||Mar-2012||Publisher:||Elsevier||Citation:||CARDOSO, Ana M. S. [et. al.] - S4(13)-PV cell-penetrating peptide induces physical and morphological changes in membrane-mimetic lipid systems and cell membranes: Implications for cell internalization. "BBA - Biomembranes". ISSN 0005-2736. 1818:3 (2012) 877-888||Serial title, monograph or event:||BBA - Biomembranes||Volume:||1818||Issue:||3||Abstract:||The present work aims to gain insights into the role of peptide–lipid interactions in the mechanisms of cellular internalization and endosomal escape of the S4(13)-PV cell-penetrating peptide, which has been successfully used in our laboratory as a nucleic acid delivery system. A S4(13)-PV analogue, S4(13)-PVscr, displaying a scrambled amino acid sequence, deficient cell internalization and drug delivery inability, was used in this study for comparative purposes. Differential scanning calorimetry, fluorescence polarization and X-ray diffraction at small and wide angles techniques showed that both peptides interacted with anionic membranes composed of phosphatidylglycerol or a mixture of this lipid with phosphatidylethanolamine, increasing the lipid order, shifting the phase transition to higher temperatures and raising the correlation length between the bilayers. However, S4(13)-PVscr, in contrast to the wild-type peptide, did not promote lipid domain segregation and induced the formation of an inverted hexagonal lipid phase instead of a cubic phase in the lipid systems assayed. Electron microscopy showed that, as opposed to S4(13)-PVscr, the wild-type peptide induced the formation of a non-lamellar organization in membranes of HeLa cells. We concluded that lateral phase separation and destabilization of membrane lamellar structure without compromising membrane integrity are on the basis of the lipid-driven and receptor-independent mechanism of cell entry of S4(13)-PV peptide. Overall, our results can contribute to a better understanding of the role of peptide–lipid interactions in the mechanisms of cell-penetrating peptide membrane translocation, helping in the future design of more efficient cell-penetrating peptide-based drug delivery systems.||URI:||http://hdl.handle.net/10316/19932||ISSN:||0005-2736||DOI:||10.1016/j.bbamem.2011.12.022||Rights:||openAccess|
|Appears in Collections:||I&D CNC - Artigos em Revistas Internacionais|
Show full item record
Files in This Item:
|S4(13)-PV cell-penetrating peptide induces physical.pdf||1.52 MB||Adobe PDF||View/Open|
checked on Feb 18, 2020
WEB OF SCIENCETM
checked on Oct 2, 2021
checked on Oct 8, 2021
checked on Oct 8, 2021
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.