Dual Control of Peptide Conformation with Light and Metal Coordination

Pritam Ghosh, Justin Torner, Paramjit S. Arora, Galia Maayan

Research output: Contribution to journalArticlepeer-review


The design of a stimuli-responsive peptide whose conformation is controlled by wavelength-specific light and metal coordination is described. The peptide adopts a defined tertiary structure and its conformation can be modulated between an α-helical coiled coil and β-sheet. The peptide is designed with a hydrophobic interface to induce coiled coil formation and is based on a recently described strategy to obtain switchable helix dimers. Herein, we endowed the helix dimer with 8-hydroxyquinoline (HQ) groups to achieve metal coordination and shift to a β-sheet structure. It was found that the conformational shift only occurs upon introduction of Zn2+; other metal ions (Cu2+, Fe3+, Co2+, Mg2, and Ni2+) do not offer switching likely due to non-specific metal-peptide coordination. A control peptide lacking the metal-coordinating residues does not show conformational switching with Zn2+ supporting the role of this metal in stabilizing the β-sheet conformation in a defined manner.

Original languageEnglish (US)
Pages (from-to)8956-8959
Number of pages4
JournalChemistry - A European Journal
Issue number35
StatePublished - Jun 21 2021


  • beta-sheet
  • coiled coils
  • coordination
  • peptides
  • photoswitches

ASJC Scopus subject areas

  • Catalysis
  • Organic Chemistry


Dive into the research topics of 'Dual Control of Peptide Conformation with Light and Metal Coordination'. Together they form a unique fingerprint.

Cite this