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Halogen Bonding: A Powerful Tool for Modulation of Peptide Conformation
University of Gothenburg, SE-41296 Gothenburg, Sweden.
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Organic Chemistry. University of Gothenburg, SE-41296 Gothenburg, Sweden.ORCID iD: 0000-0003-3798-3322
University of Gothenburg, SE-41296 Gothenburg, Sweden.
University of Gothenburg, SE-41296 Gothenburg, Sweden.
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2017 (English)In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Biochemistry, ISSN 0006-2960, Vol. 56, no 25, p. 3265-3272Article in journal (Refereed) Published
Abstract [en]

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 β-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.

Place, publisher, year, edition, pages
2017. Vol. 56, no 25, p. 3265-3272
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Organic Chemistry
Identifiers
URN: urn:nbn:se:uu:diva-346682DOI: 10.1021/acs.biochem.7b00429PubMedID: 28581720OAI: oai:DiVA.org:uu-346682DiVA, id: diva2:1191821
Available from: 2018-03-20 Created: 2018-03-20 Last updated: 2018-04-05Bibliographically approved

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