Michaela Schenk

TL;DR: The cisright harpoon over left harpoon trans photoisomerization of the azobenzene building block 4-(4-aminophenylazo)benzoic acid incorporated in a cyclic peptide facilitated a two-state transition of the peptide chain from a rigid constrained conformation in the trans isomer into the largely free conformational space of the cis isomer.

TL;DR: The search for photoresponsive conformational transitions accompanied by changes in physicochemical and biological properties led to the design of small cyclic peptides containing azobenzene moieties in the backbone, suggesting that restricted conformational freedom was already present in the monocyclic form.

TL;DR: In this article, a trans-photoisomerisierung des in ein cyclisches Peptid eingebauten Azobenzol-Bausteins 4-(4-Aminophenylazo)benzoesaure (siehe Schema) ermoglicht die Lichtschaltung eines Zwei-Zustande-Ubergangs von einer starren, konformativ eingeschrankten Struktur des trans-Isomers in den weitgehend freien Konformationsraum der

TL;DR: MD calculations served for the design of optimal ring-sizes to freeze conformationally the peptide backbone in the transisomer state and thus to amplify the effect of local topochemical changes of the lightinduced trans cis azobenzene isomerization on the conformation of the cyclic peptides.