scholarly journals Using modified aptamers for site specific protein–aptamer conjugations

2016 ◽  
Vol 7 (3) ◽  
pp. 2157-2161 ◽  
Author(s):  
Ruowen Wang ◽  
Danqing Lu ◽  
Huarong Bai ◽  
Cheng Jin ◽  
Guobei Yan ◽  
...  
Keyword(s):  
Specific Protein ◽  
New Method ◽  
Site Specific ◽  
Target Proteins ◽  
Lysine Residues

We have developed a new method for the selective conjugation of target proteins at lysine residues through a protein–aptamer template-directed reaction.

scholarly journals Site-selective enzymatic chemistry for polymer conjugation to protein lysine residues: PEGylation of G-CSF at lysine-41

2016 ◽  
Vol 7 (42) ◽  
pp. 6545-6553 ◽  
Author(s):  
A. Mero ◽  
A. Grigoletto ◽  
K. Maso ◽  
H. Yoshioka ◽  
A. Rosato ◽  
...  
Keyword(s):  
Specific Protein ◽  
Microbial Transglutaminase ◽  
Site Specific ◽  
Lysine Residues ◽  
Polymer Conjugation ◽  
Site Selective

Microbial transglutaminase (mTGase) is an enzyme that catalyzes site-specific protein derivatization at specific glutamines and lysines.

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.

scholarly journals Site-specific protein modifications through pyrroline-carboxy-lysine residues

2011 ◽  
Vol 108 (26) ◽  
pp. 10437-10442 ◽  
Author(s):  
W. Ou ◽  
T. Uno ◽  
H.-P. Chiu ◽  
J. Grunewald ◽  
S. E. Cellitti ◽  
...  
Keyword(s):  
Specific Protein ◽  
Site Specific ◽  
Protein Modifications ◽  
Lysine Residues

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>

scholarly journals Protein ubiquitination via dehydroalanine: development and insights into the diastereoselective 1,4-addition step

2016 ◽  
Vol 14 (21) ◽  
pp. 4817-4823 ◽  
Author(s):  
Roman Meledin ◽  
Sachitanand M. Mali ◽  
Sumeet K. Singh ◽  
Ashraf Brik
Keyword(s):  
Specific Protein ◽  
Site Specific ◽  
Isopeptide Bond ◽  
Protein Ubiquitination

We report a strategy for site-specific protein ubiquitination using dehydroalanine (Dha) chemistry for the preparation of ubiquitin conjugates bearing a very close mimic of the native isopeptide bond.

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