Stephan Voigt
Technische Universität Darmstadt
8 Papers
97 Citations
Stephan Voigt is an academic researcher from Technische Universität Darmstadt. The author has contributed to research in topics: Peptidomimetic & Chemistry. The author has an hindex of 5, co-authored 8 publications.
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Papers
"Triazole bridge": disulfide-bond replacement by ruthenium-catalyzed formation of 1,5-disubstituted 1,2,3-triazoles.
Martin Empting,Olga Avrutina,Reinhard Meusinger,Sebastian Fabritz,Michael Reinwarth,Markus Biesalski,Stephan Voigt,Gerd Buntkowsky,Harald Kolmar +8 more
TL;DR: The facile introduction of 1,4-disubstituted 1,2,3-triazoles into peptides and the compelling characteristics of this prototypic “click” reaction, which has been extensively applied in peptide chemistry exploiting the almost perfect orthogonality to side-chain reactivities are reported.
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Development of a Functional cis-Prolyl Bond Biomimetic and Mechanistic Implications for Nickel Superoxide Dismutase
Daniel Tietze,Marco Tischler,Stephan Voigt,Diana Imhof,Oliver Ohlenschläger,Matthias Görlach,Gerd Buntkowsky +6 more
TL;DR: The conformation of the prolyl peptide bond apparently has of minor importance for the catalytic activity of the metallopeptides as postulated in literature, and it is shown that the triazole metallopeside is forming a stable cyanide adduct as a substrate analogue model complex.
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PHIP-label: parahydrogen-induced polarization in propargylglycine-containing synthetic oligopeptides
Marco Körner,Grit Sauer,Andreas Heil,Daichi Nasu,Martin Empting,Daniel Tietze,Stephan Voigt,Heiko Weidler,Torsten Gutmann,Olga Avrutina,Harald Kolmar,Tomasz Ratajczyk,Tomasz Ratajczyk,Gerd Buntkowsky +13 more
TL;DR: The unsaturated side chain of l-propargylglycine was used to study parahydrogen-induced polarization (PHIP) in synthetic oligopeptides and for the first time PHIP-induced NMR signal enhancement was demonstrated using model peptides bearing various functional side chains.
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Revealing the Position of the Substrate in Nickel Superoxide Dismutase: A Model Study†
Daniel Tietze,Stephan Voigt,Doreen Mollenhauer,Marco Tischler,Diana Imhof,Torsten Gutmann,Leticia González,Oliver Ohlenschläger,Hergen Breitzke,Matthias Görlach,Gerd Buntkowsky +10 more
TL;DR: The investigation of a model system of the nickel superoxide dismutase (NiSOD) is able to shed light into the mode of action of this enzyme and makes it possible to decide between the proposed mechanisms.
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