Titre :

Effect of hydrophobic moment on membrane interaction and cell penetration of apolipoprotein E-derived arginine-rich amphipathic α-helical peptides

Auteur(s) :

Takechi-Haraya, Yuki [Auteur]
National Institute of Environmental Health Sciences [Durham, NC, USA] [NIEHS-NIH]
Ohgita, Takashi [Auteur]
Kotani, Mana [Auteur]
Kono, Hiroki [Auteur]
Saito, Chihiro [Auteur]
Tokyo University of Agriculture and Technology [TUAT]
Tamagaki-Asahina, Hiroko [Auteur]
Nishitsuji, Kazuchika [Auteur]
Wakayama University
Uchimura, Kenji [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Sato, Takeshi [Auteur]
Kawano, Ryuji [Auteur]
Tokyo University of Agriculture and Technology [TUAT]
Sakai-Kato, Kumiko [Auteur]
Kitasato University
Izutsu, Ken-ichi [Auteur]
National Institute of Environmental Health Sciences [Durham, NC, USA] [NIEHS-NIH]
Saito, Hiroyuki [Auteur]

Titre de la revue :

Scientific Reports

Nom court de la revue :

Sci Rep

Numéro :

12

Éditeur :

Springer Science and Business Media LLC

Date de publication :

2022-03-23

ISSN :

2045-2322

Discipline(s) HAL :

Sciences du Vivant [q-bio]

Résumé en anglais : [en]

AbstractWe previously developed an amphipathic arginine-rich peptide, A2-17, which has high ability to directly penetrate across cell membranes. To understand the mechanism of the efficient cell-penetrating ability of the ...
Lire la suite >AbstractWe previously developed an amphipathic arginine-rich peptide, A2-17, which has high ability to directly penetrate across cell membranes. To understand the mechanism of the efficient cell-penetrating ability of the A2-17 peptide, we designed three structural isomers of A2-17 having different values of the hydrophobic moment and compared their membrane interaction and direct cell penetration. Confocal fluorescence microscopy revealed that cell penetration efficiency of peptides tends to increase with their hydrophobic moment, in which A2-17 L14R/R15L, an A2-17 isomer with the highest hydrophobic moment, predominantly remains on plasma cell membranes. Consistently, Trp fluorescence analysis indicated the deepest insertion of A2-17 L14R/R15L into lipid membranes among all A2-17 isomers. Electrophysiological analysis showed that the duration and charge flux of peptide-induced pores in lipid membranes were prominent for A2-17 L14R/R15L, indicating the formation of stable membrane pores. Indeed, the A2-17 L14R/R15L peptide exhibited the strongest membrane damage to CHO-K1 cells. Atomic force microscopy quantitatively defined the peptide-induced membrane perturbation as the decrease in the stiffness of lipid vesicles, which was correlated with the hydrophobic moment of all A2-17 isomers. These results indicate that optimal membrane perturbation by amphipathic A2-17 peptide is critical for its efficient penetration into cells without inducing stabilized membrane pores.Lire moins >

Langue :

Anglais

Audience :

Internationale

Vulgarisation :

Non

Établissement(s) :

Université de Lille
CNRS

Collections :

• Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576

Équipe(s) de recherche :

Diversité structurale des héparanes sulfates et régulation de la réponse inflammatoire

Date de dépôt :

2022-11-16T15:04:54Z
2022-11-17T10:53:04Z