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The self-assembly and secondary structure of peptide amphiphiles determine the membrane permeation activity†
Rie Wakabayashi,Yuko Abe
RSC Advances Pub Date : 07/10/2014 00:00:00 , DOI:10.1039/C4RA02901A
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
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