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 4 2014
Accepted
07 7 2014
First published
10 7 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

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