Institution: | 1. Schulich Faculty of Chemistry, Technion-Israel Institute of Technology, Technion City, Haifa, 3200008 Israel
These authors contributed equally to this work.;2. Department of Chemistry, New York University, New York, New York, 10003 United States
These authors contributed equally to this work.;3. Department of Chemistry, New York University, New York, New York, 10003 United States;4. Schulich Faculty of Chemistry, Technion-Israel Institute of Technology, Technion City, Haifa, 3200008 Israel |
Abstract: | 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. |