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Photocontrolled chignolin-derived β-hairpin peptidomimetics
T Podewin1, M S Rampp, I Turkanovic
1Department of Organic Chemistry, Faculty of Chemistry and Pharmacy, Ludwig-Maximilians-University LMU, 81377 Munich, Germany. anja.hoffmann-roeder@cup.lmu.de.
Chemical Communications (Cambridge, England)
|January 28, 2015
Summary
Novel chignolin-derived peptides incorporating an azobenzene photoswitch were synthesized. These peptides exhibit reversible photoswitching, inducing folding into beta-hairpin structures, confirmed by spectroscopy.
Area of Science:
- Biochemistry
- Molecular Biology
- Materials Science
Background:
- Chignolin peptides are known for their structural properties.
- Photoswitchable molecules offer dynamic control over molecular behavior.
Purpose of the Study:
- To synthesize novel chignolin-derived peptides incorporating the azobenzene photoswitch [3-(3-aminomethyl)phenylazo]phenylacetic acid (AMPP).
- To investigate the photoswitching behavior and resulting structural changes in these novel peptides.
Main Methods:
- Peptide synthesis utilizing chignolin scaffolds.
- Incorporation of the azobenzene photoswitch (AMPP).
- Characterization using Circular Dichroism (CD), Fourier-Transform Infrared (FT-IR) spectroscopy, and Nuclear Magnetic Resonance (NMR) spectroscopy.
Main Results:
- Successful synthesis of chignolin-derived peptides containing the AMPP photoswitch.
- Demonstration of reversible photoswitching behavior upon light exposure.
- Evidence of light-induced folding into beta-hairpin-like structures.
Conclusions:
- The synthesized peptides exhibit light-responsive conformational changes.
- Azobenzene photoswitch incorporation enables controllable peptide folding.
- Spectroscopic data unequivocally confirm the formation of beta-hairpin structures.
