Thioxylation as One-Atom-Substitution Generates a Photoswitchable Element within the Peptide Backbone

The introduction of a thioxo peptide bond in agonists of the opioid μ‐receptor lead to bioactive derivatives. The backbone conformation of these compounds can be specifically modulated by photoinduction of the cis/trans prolyl bond isomerization [Eq. (1)].

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Bibliographic Details
Published inAngewandte Chemie International Edition Vol. 39; no. 6; pp. 1120 - 1122
Main Authors Frank, Robert, Jakob, Mario, Thunecke, Frank, Fischer, Gunter, Schutkowski, Mike
Format Journal Article
LanguageEnglish
Published Weinheim WILEY-VCH Verlag GmbH 17.03.2000
WILEY‐VCH Verlag GmbH
Wiley
Subjects
Chemistry
Chemistry, Multidisciplinary
endomorphines
isomerizations
peptides
photochemistry
Physical Sciences
Science & Technology
photochemistry
N-METHYLTHIOACETAMIDE
SUBSTRATE
ISOMERIZATION
peptides
BOND
endomorphines
isomerizations
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Summary:The introduction of a thioxo peptide bond in agonists of the opioid μ‐receptor lead to bioactive derivatives. The backbone conformation of these compounds can be specifically modulated by photoinduction of the cis/trans prolyl bond isomerization [Eq. (1)].
Bibliography:istex:42E32DB8F22100774DEE542797C3CA0CC2C3330F
ArticleID:ANIE1120
ark:/67375/WNG-FVJK6K8S-3
We thank Dr. Peter Bayer for the NMR investigations and Dirk Wildemann for his assistance with the peptide syntheses. This work was supported by the Deutsche Forschungsgemeinschaft, the Fond der Chemischen Industrie, the Boehringer‐Ingelheim‐Stiftung, and the Land Sachsen‐Anhalt.
ISSN:1433-7851
1521-3773
DOI:10.1002/(SICI)1521-3773(20000317)39:6<1120::AID-ANIE1120>3.0.CO;2-H