Study Findings on Cysteine Endopeptidases Are Outlined in Reports from Institute of Chemical Sciences and Engineering (A biocompatible in vivo ligation reaction and its application for noninvasive bioluminescent imaging of protease activity in ...)
By a News Reporter-Staff News Editor at Life Science Weekly -- A new study on Enzymes and Coenzymes is now available. According to news reporting originating from Lausanne, Switzerland, by NewsRx correspondents, research stated, "The discovery of biocompatible reactions had a tremendous impact on chemical biology, allowing the study of numerous biological processes directly in complex systems. However, despite the fact that multiple biocompatible reactions have been developed in the past decade, very few work well in living mice."
Our news editors obtained a quote from the research from the Institute of Chemical Sciences and Engineering, "Here we report that D-cysteine and 2-cyanobenzothiazoles can selectively react with each other in vivo to generate a luciferin substrate for firefly luciferase. The success of this 'split luciferin' ligation reaction has important implications for both in vivo imaging and biocompatible labeling strategies. First, the production of a luciferin substrate can be visualized in a live mouse by bioluminescence imaging (BLI) and furthermore allows interrogation of targeted tissues using a 'caged' luciferin approach. We therefore applied this reaction to the real-time noninvasive imaging of apoptosis associated with caspase 3/7. Caspase-dependent release of free D-cysteine from the caspase 3/7 peptide substrate Asp-Glu-Val-Asp-D-Cys (DEVD-(D-Cys)) allowed selective reaction with 6-amino-2-cyanobenzothiazole (NH(2)-CBT) in vivo to form 6-amino-D-luciferin with subsequent light emission from luciferase. Importantly, this strategy was found to be superior to the commercially available DEVD-aminoluciferin substrate for imaging of caspase 3/7 activity. Moreover, the split luciferin approach enables the modular construction of bioluminogenic sensors, where either or both reaction partners could be caged to report on multiple biological events."
According to the news editors, the research concluded: "Lastly, the luciferin ligation reaction is 3 orders of magnitude faster than Staudinger ligation, suggesting further applications for both bioluminescence and specific molecular targeting in vivo."
For more information on this research see: A biocompatible in vivo ligation reaction and its application for noninvasive bioluminescent imaging of protease activity in living mice. Acs Chemical Biology, 2013;8(5):987-99. (American Chemical Society - www.acs.org; Acs Chemical Biology - www.pubs.acs.org/journal/acbcct)
The news editors report that additional information may be obtained by contacting A. Godinat, Institute of Chemical Sciences and Engineering, Swiss Federal Institute of Technology of Lausanne, LCBIM, CH-1015 Lausanne, Switzerland. Additional authors for this research include H.M. Park, S.C. Miller, K. Cheng, D. Hanahan, L.E. Sanman, M. Bogyo, A. Yu, G.F. Nikitin, A. Stahl and E.A Dubikovskaya (see also Enzymes and Coenzymes).
Keywords for this news article include: Europe, Lausanne, Caspases, Protease, Switzerland, Luciferases, Peptide Hydrolases, Enzymes and Coenzymes, Cysteine Endopeptidases.
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