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Halogen Bonding: A Powerful Tool for Modulation of Peptide Conformation

Journal article
Authors Emma Danelius
Hanna Andersson
Patrik Jarvoll
Kajsa Lood
Jürgen Gräfenstein
Mate Erdelyi
Published in Biochemistry
Volume 56
Issue 25
Pages 3265-3272
ISSN 0006-2960
Publication year 2017
Published at Swedish NMR Centre at Göteborg University
Department of Chemistry and Molecular Biology
Pages 3265-3272
Language en
Links doi.org/10.1021/acs.biochem.7b00429
Keywords beta-hairpin stability, structural determinants, medicinal chemistry, amino-acids, protein, model, nmr, propensities, recognition, molecules, Biochemistry & Molecular Biology, nor dl, 1994, nature, v367, p660
Subject categories Organic Chemistry, Physical organic chemistry, Chemical Sciences, Biological Sciences

Abstract

Halogen bonding is a weak chemical force that has so far mostly found applications in crystal engineering. Despite its potential for use in drug discovery, as a new molecular tool in the direction of molecular recognition events, it has rarely been assessed in biopolymers. Motivated by this fact, we have developed a peptide model system that permits the quantitative evaluation of weak forces in a biologically relevant proteinlike environment and have applied it for the assessment of a halogen bond formed between two amino acid side chains. The influence of a single weak force is measured by detection of the extent to which it modulates the conformation of a cooperatively folding system. We have optimized the amino acid sequence of the model peptide on analogues with a hydrogen bond-forming site as a model for the intramolecular halogen bond to be studied, demonstrating the ability of the technique to provide information about any type of weak secondary interaction. A combined solution nuclear magnetic resonance spectroscopic and computational investigation demonstrates that an interstrand halogen bond is capable of conformational stabilization of a beta-hairpin foldamer comparable to an analogous hydrogen bond. This is the first report of incorporation of a conformation-stabilizing halogen bond into a peptide/protein system, and the first quantification of a chlorine-centered halogen bond in a biologically relevant system in solution.

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