scholarly journals Fluorogenic protein labeling using a genetically encoded unstrained alkene

2017 ◽  
Vol 8 (2) ◽  
pp. 1141-1145 ◽  
Author(s):  
X. Shang ◽  
X. Song ◽  
C. Faller ◽  
R. Lai ◽  
H. Li ◽  
...  
Keyword(s):  
Protein Labeling ◽  
Bioorthogonal Reaction

A new fluorogenic bioorthogonal reaction between styrene (an unstrained alkene) and a tetrazine was developed.

4-Halogeno-sydnones for fast strain promoted cycloaddition with bicyclo-[6.1.0]-nonyne

2014 ◽  
Vol 50 (66) ◽  
pp. 9376-9378 ◽  
Author(s):  
Lucie Plougastel ◽  
Oleksandr Koniev ◽  
Simon Specklin ◽  
Elodie Decuypere ◽  
Christophe Créminon ◽  
...  
Keyword(s):  
Click Reaction ◽  
Protein Labeling ◽  
Bioorthogonal Reaction

4-Halogeno-sydnones were found to be efficient dipole partners for the strain promoted click reaction with bicyclo-[6.1.0]-nonyne. This bioorthogonal reaction has been applied to protein labeling.

Gold labeling of teichoic acid on adjacent surfaces of staphylococcus aureus

1990 ◽  
Vol 48 (3) ◽  
pp. 578-579
Author(s):  
Margaret Hukee
Keyword(s):  
Staphylococcus Aureus ◽  
Teichoic Acid ◽  
Protein Labeling ◽  
Minimal Amount ◽  
Section Thickness ◽  
Double Labeling ◽  
Parallel Surfaces ◽  
Supporting Membrane

Gold labeling of two antigens (double labeling) is often done on two section surfaces separated by section thickness. Whether labeling is done on both sides of the same section or on two parallel surfaces separated by section thickness (PSSST), comparable results are dependent on an equal number of epitopes being exposed at each surface. We propose a method to study protein labeling within the same field of proteins, by examining two directly adjacent surfaces that were split during sectioning. The number of labeling sites on adjacent surfaces (AS) were compared to sites on PSSST surfaces in individual bacteria.Since each bacteria needed to be recognizable in all three section surfaces, one-hole grids were used for labeling. One-hole grids require a supporting membrane and excessive handling during labeling often ruptures the membrane. To minimize handling, a labeling chamber was designed that is inexpensive, disposable, minimizes contamination, and uses a minimal amount of solution.

Suzuki–Miyaura cross-coupling for chemoproteomic applications

2020 ◽  
Author(s):  
Jian Cao ◽  
Ernest Armenta ◽  
Lisa Boatner ◽  
Heta Desai ◽  
Neil Chan ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Cross Coupling ◽  
Protein Profiling ◽  
Protein Labeling ◽  
Caspase 8 ◽  
Complex Cell ◽  
Bioorthogonal Chemistry ◽  
Reaction Conditions ◽  
Target Deconvolution ◽  
Palladium Catalyzed

Bioorthogonal chemistry is a mainstay of chemoproteomic sample preparation workflows. While numerous transformations are now available, chemoproteomic studies still rely overwhelmingly on copper-catalyzed azide –alkyne cycloaddition (CuAAC) or 'click' chemistry. Here we demonstrate that gel-based activity-based protein profiling (ABPP) and mass-spectrometry-based chemoproteomic profiling can be conducted using Suzuki–Miyaura cross-coupling. We identify reaction conditions that proceed in complex cell lysates and find that Suzuki –Miyaura cross-coupling and CuAAC yield comparable chemoproteomic coverage. Importantly, Suzuki–Miyaura is also compatible with chemoproteomic target deconvolution, as demonstrated using structurally matched probes tailored to react with the cysteine protease caspase-8. Uniquely enabled by the observed orthogonality of palladium-catalyzed cross-coupling and CuAAC, we combine both reactions to achieve dual protein labeling.

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