Ionic Strength and Solution Composition Dictate the Adsorption of Cell-Penetrating Peptides onto Phosphatidylcholine Membranes.
Journal
Langmuir : the ACS journal of surfaces and colloids
ISSN: 1520-5827
Titre abrégé: Langmuir
Pays: United States
ID NLM: 9882736
Informations de publication
Date de publication:
20 09 2022
20 09 2022
Historique:
pubmed:
10
9
2022
medline:
23
9
2022
entrez:
9
9
2022
Statut:
ppublish
Résumé
Adsorption of arginine-rich positively charged peptides onto neutral zwitterionic phosphocholine (PC) bilayers is a key step in the translocation of those potent cell-penetrating peptides into the cell interior. In the past, we have shown both theoretically and experimentally that polyarginines adsorb to the neutral PC-supported lipid bilayers in contrast to polylysines. However, comparing our results with previous studies showed that the results often do not match even at the qualitative level. The adsorption of arginine-rich peptides onto 1-palmitoyl-2-oleoyl-
Identifiants
pubmed: 36083171
doi: 10.1021/acs.langmuir.2c01435
pmc: PMC9494944
doi:
Substances chimiques
Cell-Penetrating Peptides
0
Lecithins
0
Lipid Bilayers
0
Phosphatidylcholines
0
Phosphorylcholine
107-73-3
Arginine
94ZLA3W45F
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
11284-11295Références
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