Issue 13, 2015
From the journal:

Organic & Biomolecular Chemistry

Stapling monomeric GCN4 peptides allows for DNA binding and enhanced cellular uptake†

Abhishek Iyer,a   Dorien Van Lysebetten,a   Yara Ruiz García,a   Benoit Louage,b   Bruno G. De Geestb  and  Annemieke Madder*a  

* Corresponding authors

a Organic and Biomimetic Chemistry Research Group, Krijgslaan 281, S4, B-9000 Gent, Belgium
E-mail: annemieke.madder@ugent.be
Fax: +32-9-264 49 98

b Department of Pharmaceutics. Ghent University, Ottergemsesteenweg 460, 9000 Ghent, Belgium
E-mail: br.degeest@ugent.bel
Tel: +329 264 80 55

Abstract

The basic DNA recognition region of the GCN4 protein comprising 23 amino acids has been modified to contain two optimally positioned cysteines which have been linked and stapled using cross-linkers of suitable lengths. This results in stapled peptides with a stabilized α-helical conformation which allows for DNA binding and concurrent enhancement of cellular uptake.

Graphical abstract: Stapling monomeric GCN4 peptides allows for DNA binding and enhanced cellular uptake

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Article information

DOI
https://doi.org/10.1039/C4OB02659D
Article type
Communication
Submitted
24 Dec 2014
Accepted
17 Feb 2015
First published
17 Feb 2015

Org. Biomol. Chem., 2015,13, 3856-3862

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Stapling monomeric GCN4 peptides allows for DNA binding and enhanced cellular uptake

A. Iyer, D. Van Lysebetten, Y. Ruiz García, B. Louage, B. G. De Geest and A. Madder, Org. Biomol. Chem., 2015, 13, 3856 DOI: 10.1039/C4OB02659D

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