scholarly journals Strain-promoted sydnone bicyclo-[6.1.0]-nonyne cycloaddition

2014 ◽  
Vol 5 (5) ◽  
pp. 1742-1744 ◽  
Author(s):  
Stephen Wallace ◽  
Jason W. Chin
Keyword(s):  
Specific Protein ◽  
Bioorthogonal Reaction ◽  
Site Specific ◽  
Protein Labelling

We report the strain-promoted sydnone bicyclo-[6.1.0]-nonyne cycloaddition and demonstrate that this bioorthogonal reaction enables site-specific protein labelling.

scholarly journals Peptide-tags for site-specific protein labelling in vitro and in vivo

2016 ◽  
Vol 12 (6) ◽  
pp. 1731-1745 ◽  
Author(s):  
Jonathan Lotze ◽  
Ulrike Reinhardt ◽  
Oliver Seitz ◽  
Annette G. Beck-Sickinger
Keyword(s):  
Metal Ions ◽  
Small Molecules ◽  
Protein Localization ◽  
Specific Protein ◽  
Site Specific ◽  
Protein Labelling ◽  
Peptide Interactions ◽  
Peptide Tags

Peptide-tag based labelling can be achieved by (i) enzymes (ii) recognition of metal ions or small molecules and (iii) peptide–peptide interactions and enables site-specific protein visualization to investigate protein localization and trafficking.

scholarly journals Genetically encoded norbornene directs site-specific cellular protein labelling via a rapid bioorthogonal reaction

2012 ◽  
Vol 4 (4) ◽  
pp. 298-304 ◽  
Author(s):  
Kathrin Lang ◽  
Lloyd Davis ◽  
Jessica Torres-Kolbus ◽  
Chungjung Chou ◽  
Alexander Deiters ◽  
...  
Keyword(s):  
Cellular Protein ◽  
Bioorthogonal Reaction ◽  
Site Specific ◽  
Protein Labelling

scholarly journals Site-specific protein labelling and immobilization mediated by microbial transglutaminase

2014 ◽  
Vol 50 (50) ◽  
pp. 6604-6606 ◽  
Author(s):  
Samuel K. Oteng-Pabi ◽  
Christophe Pardin ◽  
Maria Stoica ◽  
Jeffrey W. Keillor
Keyword(s):  
Specific Protein ◽  
Microbial Transglutaminase ◽  
Site Specific ◽  
Protein Labelling ◽  
Target Proteins ◽  
Subsequent Modification

Microbial transglutaminase (mTG) mediates site-specific propargylation of target proteins, allowing their subsequent modification in in vitro bio-conjugation applications.

Systematic Engineering of a Protein Nanocage for High-Yield, Site-Specific Modification

2018 ◽  
Author(s):  
Daniel D. Brauer ◽  
Emily C. Hartman ◽  
Daniel L.V. Bader ◽  
Zoe N. Merz ◽  
Danielle Tullman-Ercek ◽  
...  
Keyword(s):  
Small Molecules ◽  
Protein Modification ◽  
Positive Charge ◽  
Specific Protein ◽  
High Yield ◽  
Site Specific ◽  
Protein Cage ◽  
Protein Carriers ◽  
Site Selective ◽  
Targeted Library

<div> <p>Site-specific protein modification is a widely-used strategy to attach drugs, imaging agents, or other useful small molecules to protein carriers. N-terminal modification is particularly useful as a high-yielding, site-selective modification strategy that can be compatible with a wide array of proteins. However, this modification strategy is incompatible with proteins with buried or sterically-hindered N termini, such as virus-like particles like the well-studied MS2 bacteriophage coat protein. To assess VLPs with improved compatibility with these techniques, we generated a targeted library based on the MS2-derived protein cage with N-terminal proline residues followed by three variable positions. We subjected the library to assembly, heat, and chemical selections, and we identified variants that were modified in high yield with no reduction in thermostability. Positive charge adjacent to the native N terminus is surprisingly beneficial for successful extension, and over 50% of the highest performing variants contained positive charge at this position. Taken together, these studies described nonintuitive design rules governing N-terminal extensions and identified successful extensions with high modification potential.</p> </div>

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