Phospha-Scorpionate Complexes by Click Chemistry using Phenyl Azide and Ethynylphosphine Oxides

2008 ◽  
Vol 27 (13) ◽  
pp. 3210-3215 ◽  
Author(s):  
Sander G. A. van Assema ◽  
Cornelis G. J. Tazelaar ◽  
G. Bas de Jong ◽  
Jan H. van Maarseveen ◽  
Marius Schakel ◽  
...  
Keyword(s):  
Click Chemistry ◽  
Phenyl Azide

scholarly journals Functional modulation and directed assembly of an enzyme through designed non-natural post-translation modification

2015 ◽  
Vol 6 (7) ◽  
pp. 3712-3717 ◽  
Author(s):  
Andrew M. Hartley ◽  
Athraa J. Zaki ◽  
Adam R. McGarrity ◽  
Cecile Robert-Ansart ◽  
Andriy V. Moskalenko ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Click Chemistry ◽  
Directed Assembly ◽  
Phenyl Azide ◽  
Functional Modulation

Designed phenyl azide incorporation combined with bioorthogonal Click chemistry to regulate enzyme activity, or promote its stable assembly on graphene.

Bis(pentafluorosulfanyl)phenyl Azide as an Expeditious Tool for Click Chemistry toward Antitumor Pharmaceuticals

ChemMedChem ◽  
2014 ◽  
Vol 9 (5) ◽  
pp. 913-917 ◽  
Author(s):  
Yu-Dong Yang ◽  
Etsuko Tokunaga ◽  
Hidehiko Akiyama ◽  
Norimichi Saito ◽  
Norio Shibata
Keyword(s):  
Click Chemistry ◽  
Phenyl Azide

Click Chemistry Expedited Radiosynthesis: Sulfur [18F]fluoride Exchange of Aryl Fluorosulfates

2019 ◽  
Author(s):  
Qinheng Zheng ◽  
Hongtao Xu ◽  
Hua Wang ◽  
Wen-Ge Han Du ◽  
Nan Wang ◽  
...  
Keyword(s):  
Click Chemistry ◽  
High Performance ◽  
Isotopic Exchange ◽  
Tumor Imaging ◽  
Radiochemical Yield ◽  
Exchange Method ◽  
Molar Activity ◽  
Positron Emission ◽  
Sulfur Fluoride

The lack of simple, efficient [<sup>18</sup>F]fluorination processes and new target-specific organofluorine probes remains the major challenge of fluorine-18-based positron emission tomography (PET). We report here a fast isotopic exchange method for the radiosynthesis of aryl [<sup>18</sup>F]fluorosulfate based PET agents enabled by the emerging sulfur fluoride exchange (SuFEx) click chemistry. The method has been applied to the fully-automated <sup>18</sup>F-radiolabeling of twenty-five structurally diverse aryl fluorosulfates with excellent radiochemical yield (83–100%) and high molar activity (up to 281 GBq µmol<sup>–1</sup>) at room temperature in 30 seconds. The purification of radiotracers requires no time-consuming high-performance liquid chromatography (HPLC), but rather a simple cartridge filtration. The utility of aryl [<sup>18</sup>F]fluorosulfate is demonstrated by the <i>in vivo</i> tumor imaging by targeting poly(ADP-ribose) polymerase 1 (PARP1).

Site-Specific Protein Covalent Attachment to Nanotubes and Its Electronic Impact on Single Molecule Function

2019 ◽  
Author(s):  
Adam Beachey ◽  
Harley Worthy ◽  
William David Jamieson ◽  
Suzanne Thomas ◽  
Benjamin Bowen ◽  
...  
Keyword(s):  
Single Molecule ◽  
Fluorescent Protein ◽  
Functional Integration ◽  
Attachment Site ◽  
Covalent Attachment ◽  
Great Promise ◽  
Functional Coupling ◽  
Phenyl Azide ◽  
Electronic Impact ◽  
Protein Attachment

<p>Functional integration of proteins with carbon-based nanomaterials such as nanotubes holds great promise in emerging electronic and optoelectronic applications. Control over protein attachment poses a major challenge for consistent and useful device fabrication, especially when utilizing single/few molecule properties. Here, we exploit genetically encoded phenyl azide photochemistry to define the direct covalent attachment of three different proteins, including the fluorescent protein GFP, to carbon nanotube side walls. Single molecule fluorescence revealed that on attachment to SWCNTs GFP’s fluorescence changed in terms of intensity and improved resistance to photobleaching; essentially GFP is fluorescent for much longer on attachment. The site of attachment proved important in terms of electronic impact on GFP function, with the attachment site furthest from the functional center having the larger effect on fluorescence. Our approach provides a versatile and general method for generating intimate protein-CNT hybrid bioconjugates. It can be potentially applied easily to any protein of choice; attachment position and thus interface characteristics with the CNT can easily be changed by simply placing the phenyl azide chemistry at different residues by gene mutagenesis. Thus, our approach will allow consistent construction and modulate functional coupling through changing the protein attachment position.</p>

Use of Click-Chemistry in the Development of Peptidomimetic Enzyme Inhibitors

2014 ◽  
Vol 21 (13) ◽  
pp. 1467-1477 ◽  
Author(s):  
P. Fabbrizzi ◽  
G. Menchi ◽  
A. Guarna ◽  
A. Trabocchi
Keyword(s):  
Click Chemistry ◽  
Enzyme Inhibitors
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