Loading…

Noncationic Rigid and Anisotropic Coiled-Coil Proteins Exhibit Cell-Penetration Activity

Numerous cationic peptides that penetrate cells have been studied intensively as drug delivery system carriers for cellular delivery. However, cationic molecules tend to be cytotoxic and cause inflammation, and their stability in the blood is usually low. We have previously demonstrated that a rigid...

Full description

Saved in:
Bibliographic Details
Published in:Langmuir 2015-08, Vol.31 (30), p.8218-8223
Main Authors: Nakayama, Norihisa, Hagiwara, Kyoji, Ito, Yoshihiro, Ijiro, Kuniharu, Osada, Yoshihito, Sano, Ken-Ichi
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Numerous cationic peptides that penetrate cells have been studied intensively as drug delivery system carriers for cellular delivery. However, cationic molecules tend to be cytotoxic and cause inflammation, and their stability in the blood is usually low. We have previously demonstrated that a rigid and fibrous cationic coiled-coil protein exhibited cell-penetrating ability superior to that of previously reported cell-penetrating peptides. Making use of structural properties, here we describe the cell-penetrating activity of a rigid and fibrous coiled-coil protein with a noncationic surface. A fibrous coiled-coil protein of pI 6.5 penetrated 100% of the cells tested in vitro at a concentration of 500 nM, which is comparable to that of previously reported cell-penetrating peptides. We also investigated the effect of cell-strain dependency and short-term cytotoxicity.
ISSN:0743-7463
1520-5827
DOI:10.1021/acs.langmuir.5b01219