Coiled-Coil Peptide Beacon: A Tunable Conformational Switch for Protein Detection

Carolin Mueller, Tom N. Grossmann

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

The understanding of protein folding and assembly is of central importance for the design of proteins and enzymes with novel or improved functions. Minimalistic model systems, such as coiled-coils, provide an excellent platform to improve this understanding and to construct novel molecular devices. Along those lines, we designed a conformational switch that is composed of two coiled-coil forming peptides and a central binding epitope. In the absence of a binding partner, this switch adopts a hairpin-like conformation that opens upon receptor binding. Variation of the coiled-coil length modulates the strength of the intramolecular constraint. The two conformational states of this switch have been linked with characteristic fluorescent properties, which enables the detection of the receptor in real-time.

Original languageEnglish
Pages (from-to)17079-17083
Number of pages5
JournalAngewandte Chemie - International Edition
Volume57
Issue number52
Early online date9 Nov 2018
DOIs
Publication statusPublished - 21 Dec 2018

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Peptides
Switches
Proteins
Epitopes
Protein folding
Conformations
Enzymes

Keywords

  • conformational constraint
  • heterodimeric coiled-coil
  • molecular beacons
  • molecular devices
  • protein–protein interactions

Cite this

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Coiled-Coil Peptide Beacon : A Tunable Conformational Switch for Protein Detection. / Mueller, Carolin; Grossmann, Tom N.

In: Angewandte Chemie - International Edition, Vol. 57, No. 52, 21.12.2018, p. 17079-17083.

Research output: Contribution to JournalArticleAcademicpeer-review

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