scholarly journals Allyl Sulfides Are Privileged Substrates in Aqueous Cross-Metathesis: Application to Site-Selective Protein Modification

2008 ◽  
Vol 130 (30) ◽  
pp. 9642-9643 ◽  
Author(s):  
Yuya A. Lin ◽  
Justin M. Chalker ◽  
Nicola Floyd ◽  
Gonçalo J. L. Bernardes ◽  
Benjamin G. Davis
Keyword(s):  
Protein Modification ◽  
Cross Metathesis ◽  
Site Selective ◽  
Allyl Sulfides

ChemInform Abstract: Allyl Sulfides Are Privileged Substrates in Aqueous Cross-Metathesis: Application to Site-Selective Protein Modification.

ChemInform ◽  
2008 ◽  
Vol 39 (49) ◽  
Author(s):  
Yuya A. Lin ◽  
Justin M. Chalker ◽  
Nicola Floyd ◽  
Goncalo J. L. Bernardes ◽  
Benjamin G. Davis
Keyword(s):  
Protein Modification ◽  
Cross Metathesis ◽  
Site Selective ◽  
Allyl Sulfides

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>

Synthesis of Conjugated Triynes via Alkyne Metathesis

2019 ◽  
Author(s):  
Idriss Curbet ◽  
Sophie Colombel-Rouen ◽  
Romane Manguin ◽  
Anthony Clermont ◽  
Alexandre Quelhas ◽  
...  
Keyword(s):  
Steric Hindrance ◽  
High Selectivity ◽  
Alkyne Metathesis ◽  
Cross Metathesis ◽  
Synthetic Strategy ◽  
Sterically Hindered ◽  
Site Selective

<div> <div> <div> <div> <p>The synthesis of conjugated triynes by molybdenum-catalyzed alkyne metathesis is reported. Strategic to the success of this approach is the utilization of sterically-hindered diynes that allowed for the site- selective alkyne metathesis to produce the desired con- jugated triyne products. The steric hindrance of alkyne moiety was found to be crucial in preventing the for- mation of diyne byproducts. This novel synthetic strategy was amenable to self- and cross-metathesis providing straightforward access to the corresponding symmetrical and dissymmetrical triynes with high selectivity. </p> </div> </div> </div> </div>

scholarly journals Site-selective protein-modification chemistry for basic biology and drug development

2015 ◽  
Vol 8 (2) ◽  
pp. 103-113 ◽  
Author(s):  
Nikolaus Krall ◽  
Filipa P. da Cruz ◽  
Omar Boutureira ◽  
Gonçalo J. L. Bernardes
Keyword(s):  
Drug Development ◽  
Protein Modification ◽  
Basic Biology ◽  
Site Selective

Tyrosine-Triazolinedione Bioconjugation as Site-Selective Protein Modification Starting from RAFT-Derived Polymers

2017 ◽  
Vol 6 (12) ◽  
pp. 1368-1372 ◽  
Author(s):  
Stef Vandewalle ◽  
Ruben De Coen ◽  
Bruno G. De Geest ◽  
Filip E. Du Prez
Keyword(s):  
Protein Modification ◽  
Site Selective
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