Issue 37, 2016

Introduction of a tailor made anion receptor into the side chain of small peptides allows fine-tuning the thermodynamic signature of peptide–DNA binding

Abstract

The binding between peptides and DNA is often driven by entropic forces. We demonstrate herein a new approach to shift the thermodynamic profile of peptide/DNA binding from entropy to enthalpy driven. This eventually leads to higher compacted DNA aggregates which are important for gene transfection.

Graphical abstract: Introduction of a tailor made anion receptor into the side chain of small peptides allows fine-tuning the thermodynamic signature of peptide–DNA binding

Supplementary files

Article information

Article type
Paper
Submitted
25 Jul 2016
Accepted
26 Aug 2016
First published
26 Aug 2016

Org. Biomol. Chem., 2016,14, 8800-8803

Introduction of a tailor made anion receptor into the side chain of small peptides allows fine-tuning the thermodynamic signature of peptide–DNA binding

M. Li, S. Schlesiger, S. K. Knauer and C. Schmuck, Org. Biomol. Chem., 2016, 14, 8800 DOI: 10.1039/C6OB01584K

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