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A photoinducible beta-hairpin
Andreas Aemissegger1, Vincent Kräutler, Wilfred F van Gunsteren
1Laboratorium für Organische Chemie and Laboratorium für Physikalische Chemie, Swiss Federal Institute of Technology, ETH-Hönggerberg, CH-8093 Zürich, Switzerland. hilvert@org.chem.ethz.ch
Journal of the American Chemical Society
|March 3, 2005
Summary
Researchers used a photochromic azobenzene linker to control beta-hairpin peptide folding. Light-induced changes to the linker enabled well-defined beta-hairpin structures, offering insights into peptide folding and stability.
Area of Science:
- Biochemistry
- Molecular Biology
- Photochemistry
Background:
- Beta-hairpins are crucial secondary structures in proteins.
- Controlling peptide folding is essential for understanding protein structure-function relationships.
- Photochromic molecules offer light-inducible control over molecular conformation.
Purpose of the Study:
- To incorporate a photochromic azobenzene linker into a beta-hairpin peptide.
- To investigate the effect of the linker's conformation on peptide folding.
- To determine if light could be used to induce and stabilize beta-hairpin structures.
Main Methods:
- Synthesis of an azobenzene-containing peptide.
- Spectroscopic analysis, including (1)H NMR, to determine structure.
- Photoisomerization studies to assess linker dynamics.
Main Results:
- The trans isomer of the azobenzene linker promoted oligomer formation, hindering structure determination.
- Irradiation to the cis isomer induced monomer formation and a well-defined beta-hairpin structure.
- The isomerization rate of the azobenzene-containing peptide was slightly slower than the unsubstituted chromophore.
Conclusions:
- Photochromic azobenzene linkers can act as photoinducible turn elements in peptides.
- Light can be used to control beta-hairpin folding and stability.
- This approach provides a method to investigate and manipulate peptide secondary structures.