Jump to main content
Jump to site search


Short oligoalanine helical peptides for supramolecular nanopore assembly and protein cytosolic delivery

Author affiliations

Abstract

In this work we report a rational design strategy for the identification of new peptide prototypes for the non-disruptive supramolecular permeation of membranes and the transport of different macromolecular giant cargos. The approach targets a maximal enhancement of helicity in the presence of membranes with sequences bearing the minimal number of cationic and hydrophobic moieties. The here reported folding enhancement in membranes allowed the selective non-lytic translocation of different macromolecular cargos including giant proteins. The transport of different high molecular weight polymers and functional proteins was demonstrated in vesicles and in cells with excellent efficiency and optimal viability. As a proof of concept, functional monoclonal antibodies were transported for the first time into different cell lines and cornea tissues by exploiting the helical control of a short peptide sequence. This work introduces a rational design strategy that can be employed to minimize the number of charges and hydrophobic residues of short peptide carriers to achieve non-destructive transient membrane permeation and transport of different macromolecules.

Graphical abstract: Short oligoalanine helical peptides for supramolecular nanopore assembly and protein cytosolic delivery

Back to tab navigation

Supplementary files

Article information


Submitted
19 Jun 2020
Accepted
07 Nov 2020
First published
08 Dec 2020

This article is Open Access

RSC Chem. Biol., 2021, Advance Article
Article type
Paper

Short oligoalanine helical peptides for supramolecular nanopore assembly and protein cytosolic delivery

M. Pazo, G. Salluce, I. Lostalé-Seijo, M. Juanes, F. Gonzalez, R. Garcia-Fandiño and J. Montenegro, RSC Chem. Biol., 2021, Advance Article , DOI: 10.1039/D0CB00103A

This article is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported Licence. Material from this article can be used in other publications provided that the correct acknowledgement is given with the reproduced material and it is not used for commercial purposes.

Reproduced material should be attributed as follows:

  • For reproduction of material from NJC:
    [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the Centre National de la Recherche Scientifique (CNRS) and the RSC.
  • For reproduction of material from PCCP:
    [Original citation] - Published by the PCCP Owner Societies.
  • For reproduction of material from PPS:
    [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the European Society for Photobiology, the European Photochemistry Association, and RSC.
  • For reproduction of material from all other RSC journals:
    [Original citation] - Published by The Royal Society of Chemistry.

Information about reproducing material from RSC articles with different licences is available on our Permission Requests page.


Social activity

Search articles by author

Spotlight

Advertisements