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Literature DB >> 26356324

Bioorthogonal Enzymatic Activation of Caged Compounds.

Cornelia Ritter¹, Nathalie Nett¹, Carlos G Acevedo-Rocha^1,2,3,4, Richard Lonsdale^1,2, Katja Kräling¹, Felix Dempwolff³, Sabrina Hoebenreich¹, Peter L Graumann^1,3, Manfred T Reetz^5,6, Eric Meggers^7,8.

Abstract

Engineered cytochrome P450 monooxygenase variants are reported as highly active and selective catalysts for the bioorthogonal uncaging of propargylic and benzylic ether protected substrates, including uncaging in living E. coli. observed selectivity is supported by induced-fit docking and molecular dynamics simulations. This proof-of-principle study points towards the utility of bioorthogonal enzyme/protecting group pairs for applications in the life sciences.

Entities: Chemical Species

Keywords: bioorthogonal chemistry; cytochromes; directed evolution; protecting groups; protein engineering

Mesh：

Substances：

Year: 2015 PMID： 26356324 DOI： 10.1002/anie.201506739

Source DB: PubMed Journal: Angew Chem Int Ed Engl ISSN： 1433-7851 Impact factor: 15.336

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Cited

8 in total

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Bioorthogonal Enzymatic Activation of Caged Compounds.

Review 1. Development and application of bond cleavage reactions in bioorthogonal chemistry.

Review 2. The development of anticancer ruthenium(ii) complexes: from single molecule compounds to nanomaterials.

3. A DNAzyme-augmented bioorthogonal catalysis system for synergistic cancer therapy.

4. Rapid Bioorthogonal Chemistry Turn-on through Enzymatic or Long Wavelength Photocatalytic Activation of Tetrazine Ligation.

5. Bioorthogonal catalytic nanozyme-mediated lysosomal membrane leakage for targeted drug delivery.

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