Curvature Engineering: Positive Membrane Curvature Induced by Epsin N-Terminal Peptide Boosts Internalization of Octaarginine

被引：53

作者：

Pujals, Silvia ^{[1
]}

Miyamae, Hiroki ^{[1
]}

Afonin, Sergii ^{[2
]}

Murayama, Tomo ^{[1
]}

Hirose, Hisaaki ^{[1
]}

Nakase, Ikuhiko ^{[1
]}

Taniuchi, Kentaro ^{[5
]}

Umeda, Masato ^{[5
]}

Sakamoto, Kazutami

Ulrich, Anne S. ^{[2
,3
,4
,6
]}

Futaki, Shiroh ^{[1
]}

机构：

[1] Kyoto Univ, Inst Chem Res, Kyoto 6110011, Japan

[2] Karlsruhe Inst Technol, Inst Biol Interfaces IBG 2, D-76021 Karlsruhe, Germany

[3] Karlsruhe Inst Technol, Inst Organ Chem, D-76131 Karlsruhe, Germany

[4] Karlsruhe Inst Technol, CFN, D-76131 Karlsruhe, Germany

[5] Kyoto Univ, Grad Sch Engn, Dept Synthet Chem & Biol Chem, Nishikyo Ku, Kyoto 6158510, Japan

[6] Chiba Inst Sci, Choshi, Chiba 2880025, Japan

来源：

ACS CHEMICAL BIOLOGY | 2013年 / 8卷 / 09期

关键词：

CELL-PENETRATING PEPTIDES; ARGININE-RICH PEPTIDES; DOMAIN; MECHANISMS; DELIVERY; TRANSLOCATION; BINDING; PORES;

D O I：

10.1021/cb4002987

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Epsin-1 is a representative protein for inducing the positive curvature necessary for the formation of clathrin-coated pits. Here we demonstrate that the N-terminus 18-residue peptide of epsin-1 (EpN18) has this ability per se, as proved by differential scanning calorimetry (DSC) and solid-state NMR. Moreover, it is shown how this positive curvature promotion can be exploited for promoting the direct penetration of a representative cell-penetrating peptide (CPP), octaarginine (R-8), through artificial and plasma membranes. This synergistic effect has been used for the efficient delivery of a proapoptotic domain peptide (PAD), which induced high level of apoptosis only when coadministered with R-8 and EpN18, thus emphasizing the importance of positive curvature induction for achieving the desired ultimate cargo bioavailability.

引用

页码：1894 / 1899

页数：6

共 34 条

[1] The cell-penetrating peptide TAT(48-60) induces a non-lamellar phase in DMPC membranes [J].