"Ultrafast conformational dynamics in cyclic azobenzene peptides of increased flexibility"J. Wachtveitl, S. Spörlein, H. Satzger, B. Fonrobert, C. Renner, R. Behrendt, D. Oesterhelt, L. Moroder, W. Zinth
Biophys. J. 86 (2004) 2350-2362
Structural changes of peptides containing the azobenzene dye 4-aminomethyl-phenylazobenzoic acid (AMPB) are studied with ultrafast spectroscopy. AMPB peptides are a new class of molecules where the photoisomerizable dye azobenzene is linked to the peptide moiety via a exible methylene spacer. The ultrafast reactions in the femtosecond to nanosecond time domain are investigated for the optical switch AMPB, a linear and cyclic octapeptide, and a bicyclic octapeptide containing an additional disul de bridge. These molecules with increasing conformational constraints are studied for the cis to trans and the trans to cis photoreactions. For the cis to trans reaction the isomerization of the chromophore occurs fast in the 1-ps range, whereas it is slower (10-ps range) in the trans to cis reaction. In all peptides the structural changes of the chromophore lead to modi cations in the peptide structure in the 10-ps 1-ns time range. The results indicate that the chromophore AMPB acts simultaneously as a fast molecular switch and as a sensor for initial conformational dynamics in the peptide. Experiments in the mid-infrared range where the structural changes of the peptide backbone are directly observed demonstrate that the essential part of the structural dynamics in the bicyclic AMPB peptide occurs faster than 10 ns.
BMO authors (in alphabetic order):
Peptide and protein folding
Photoswitchable model peptides and their conformational dynamics