Issue 58, 2014

The self-assembly and secondary structure of peptide amphiphiles determine the membrane permeation activity

Abstract

Membrane fusogenic peptides have attracted increasing attention because of their unique biofunctions in membrane translocation and viral infection. Here, we designed GALA-related peptides with palmitoyl tails. Our study indicated that the self-assembling propensity and the secondary structure of these peptide amphiphiles greatly influenced the membrane permeability.

Graphical abstract: The self-assembly and secondary structure of peptide amphiphiles determine the membrane permeation activity

Supplementary files

Article information

Article type
Communication
Submitted
02 apr 2014
Accepted
07 jul 2014
First published
10 jul 2014

RSC Adv., 2014,4, 30654-30657

The self-assembly and secondary structure of peptide amphiphiles determine the membrane permeation activity

R. Wakabayashi, Y. Abe, N. Kamiya and M. Goto, RSC Adv., 2014, 4, 30654 DOI: 10.1039/C4RA02901A

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements