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000022704 084__ $$2WoS$$aBiochemical Research Methods
000022704 084__ $$2WoS$$aSpectroscopy
000022704 1001_ $$0P:(DE-HGF)0$$aDeeg, A.A.$$b0
000022704 245__ $$aAmyloid-Like Structures Formed by Azobenzene Peptides: Light-Triggered Disassembly
000022704 260__ $$aSpringfield, Or.$$bAster Pub. Corp.$$c2012
000022704 300__ $$a387 - 391
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000022704 500__ $$aThe work was supported by the German Science Foundation, SFB 749, and the Munich Center of Integrated Protein Science, CIPSM. The University of Zurich did not contribute to this work.
000022704 520__ $$aThe 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 relaxation of vibrational excess energy (heat) or to structural rearrangements of isomerized azobenzene and the aggregated surroundings. It is only on the time scale of minutes that spectral signatures appear which are characteristic for the disassembly of the aggregated structure.
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000022704 65320 $$2Author$$aamyloid-disassembly
000022704 65320 $$2Author$$aazobenzene
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000022704 65320 $$2Author$$atime-resolved-vibrational spectroscopy
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