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Hindawi Publishing Corporation Spectroscopy: An International Journal Volume 27 (2012), Issue 5-6, Pages 387–391 doi:10.1155/2012/108959 Amyloid-Like Structures Formed by Azobenzene Peptides: Light-Triggered Disassembly Andreas A. Deeg,1 Tobias E. Schrader,2 Halina Strzalka,1, 3 Jose Pfizer,4 Luis Moroder,4 and Wolfgang Zinth1 1 Institute of BioMolecular Optics and Munich Center of Integrated Protein Science (CIPSM), Ludwig-Maximilians-University, 80538 Munich, Germany 2 Julich Centre for Neutron Science (JCNS), Forschungszentrum Julich GmbH Outstation at FRM II, ¨ ¨ 85747 Garching, Germany 3 Physical Chemistry Institute, University of Zurich, 8057 Zurich, Switzerland ¨ 4 Max Planck Institute of Biochemistry, 82152 Martinsried, Germany Correspondence should be addressed to Andreas A. Deeg, andreas.deeg@physik.uni-muenchen.de Copyright © 2012 Andreas A. Deeg et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Abstract. The light-driven disassembly process of amyloid-like structures formed by azobenzene model peptides is studied by time-resolved mid-IR spectroscopy from nanoseconds to minutes. The investigated peptide consists of two amino acid strands connected by the azobenzene switch. The peptides aggregate to amyloid-like structures when the azobenzene chromophore is in the trans-conformation. Illumination, resulting in a trans- to cis-isomerization of the azobenzene, leads to disaggregation of the aggregated structures. After optical excitation and isomerization of the azobenzene, one finds absorption changes which recover to a large extent on the time scale of few nanoseconds. These early absorption transients are assigned to the