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Halogen Bonding: A Powerful Tool for Modulation of Peptide Conformation

Artikel i vetenskaplig tidskrift
Författare Emma Danelius
Hanna Andersson
Patrik Jarvoll
Kajsa Lood
Jürgen Gräfenstein
Mate Erdelyi
Publicerad i Biochemistry
Volym 56
Nummer/häfte 25
Sidor 3265-3272
ISSN 0006-2960
Publiceringsår 2017
Publicerad vid Svenskt NMR-centrum vid Göteborgs universitet
Institutionen för kemi och molekylärbiologi
Sidor 3265-3272
Språk English
Länkar doi.org/10.1021/acs.biochem.7b00429
Ämnesord beta-hairpin stability, structural determinants, medicinal chemistry, amino-acids, protein, model, nmr, propensities, recognition, molecules, Biochemistry & Molecular Biology, nor dl, 1994, nature, v367, p660
Ämneskategorier Biologiska vetenskaper, Kemi

Sammanfattning

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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