Derivatization of Antibody Fab Fragments: A Designer Enzyme for Native Protein Modification

ChemBioChem ◽  
2014 ◽  
Vol 15 (8) ◽  
pp. 1096-1100 ◽  
Author(s):  
Sandra Liebscher ◽  
Petra Kornberger ◽  
Gerhard Fink ◽  
Eva-Maria Trost-Gross ◽  
Eva Höss ◽  
...  
Keyword(s):  
Protein Modification ◽  
Native Protein ◽  
Fab Fragments

Traceless and Chemoselective Amine Bioconjugation via Phthalimidine Formation in Native Protein Modification

2016 ◽  
Vol 18 (11) ◽  
pp. 2600-2603 ◽  
Author(s):  
Chun Ling Tung ◽  
Clarence T. T. Wong ◽  
Eva Yi Man Fung ◽  
Xuechen Li
Keyword(s):  
Protein Modification ◽  
Native Protein

scholarly journals Selective modification of a native protein in a patient tissue homogenate using palladium nanoparticles

2019 ◽  
Vol 55 (100) ◽  
pp. 15121-15124 ◽  
Author(s):  
Arnaud Peramo ◽  
Anaëlle Dumas ◽  
Hynd Remita ◽  
Mireille Benoît ◽  
Stephanie Yen-Nicolay ◽  
...  
Keyword(s):  
Palladium Nanoparticles ◽  
Protein Modification ◽  
Tissue Homogenate ◽  
Native Protein

A chemoselective native protein modification in near-organ medium was achieved using new benign palladium nanoparticles.

Chemoselective and site-selective peptide and native protein modification enabled by aldehyde auto-oxidation

2017 ◽  
Vol 53 (5) ◽  
pp. 959-962 ◽  
Author(s):  
Landa Purushottam ◽  
Srinivasa Rao Adusumalli ◽  
Maheshwerreddy Chilamari ◽  
Vishal Rai
Keyword(s):  
Protein Modification ◽  
Lysine Residue ◽  
Chemical Technology ◽  
Single Site ◽  
Native Protein ◽  
Protein Backbone ◽  
Precision Engineering ◽  
One Pot ◽  
Site Selective

Chemical technology delivers precision engineering of the native protein backbone. A lysine residue undergoes single-site formylation or acylation in a multi-step yet operationally simple one-pot process.

De Novo Development of a Universal Biosensing Platform by Rapid Direct Native Protein Modification

2021 ◽  
Vol 93 (12) ◽  
pp. 5291-5300
Author(s):  
Xinyi Hua ◽  
Zhifang Wang ◽  
Ziqi Wang ◽  
Linlin Chen ◽  
Zaichun Zhou ◽  
...  
Keyword(s):  
Protein Modification ◽  
De Novo ◽  
Native Protein

Large-cluster and combined fluorescent and gold immunoprobes

1996 ◽  
Vol 54 ◽  
pp. 892-893
Author(s):  
Richard D. Powell ◽  
James F. Hainfeld ◽  
Carol M. R. Halsey ◽  
David L. Spector ◽  
Shelley Kaurin ◽  
...  
Keyword(s):  
Metal Cluster ◽  
Sulfonyl Chloride ◽  
Gel Filtration ◽  
Cross Linking ◽  
Site Specific ◽  
Fab Fragments ◽  
Cluster Label ◽  
Covalently Linked ◽  
Texas Red ◽  
Fold Excess

Two new types of covalently linked, site-specific immunoprobes have been prepared using metal cluster labels, and used to stain components of cells. Combined fluorescein and 1.4 nm “Nanogold” labels were prepared by using the fluorescein-conjugated tris (aryl) phosphine ligand and the amino-substituted ligand in the synthesis of the Nanogold cluster. This cluster label was activated by reaction with a 60-fold excess of (sulfo-Succinimidyl-4-N-maleiniido-cyclohexane-l-carboxylate (sulfo-SMCC) at pH 7.5, separated from excess cross-linking reagent by gel filtration, and mixed in ten-fold excess with Goat Fab’ fragments against mouse IgG (obtained by reduction of F(ab’)2 fragments with 50 mM mercaptoethylamine hydrochloride). Labeled Fab’ fragments were isolated by gel filtration HPLC (Superose-12, Pharmacia). A combined Nanogold and Texas Red label was also prepared, using a Nanogold cluster derivatized with both and its protected analog: the cluster was reacted with an eight-fold excess of Texas Red sulfonyl chloride at pH 9.0, separated from excess Texas Red by gel filtration, then deprotected with HC1 in methanol to yield the amino-substituted label.

Unrestrictive protein modification localization and quality control for open search of mass spectra

2018 ◽  
Author(s):  
Zhiwu An ◽  
Fuzhou Gong ◽  
Yan Fu
Keyword(s):  
Mass Spectrometry ◽  
Quality Control ◽  
Tandem Mass Spectrometry ◽  
Mass Spectra ◽  
Protein Modification ◽  
Software Tool ◽  
Tandem Mass ◽  
Simulation Data ◽  
Post Translational Modifications

We have developed PTMiner, a first software tool for automated, confident filtering, localization and annotation of protein post-translational modifications identified by open (mass-tolerant) search of large tandem mass spectrometry datasets. The performance of the software was validated on carefully designed simulation data. <br>

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>

Potassium Arylethynyltrifluoroborate as an Unstrained Dienophile for Ultrafast and On Demand Activation of Bioorthogonal IEDDA Reactions

2019 ◽  
Author(s):  
Zijian Guo ◽  
Bruno Oliveira ◽  
Claudio D. Navo ◽  
Pedro M. S. D. Cal ◽  
Francisco Corzana ◽  
...  
Keyword(s):  
Protein Modification ◽  
Cross Reactivity ◽  
Diels Alder ◽  
Inverse Electron Demand ◽  
On Demand ◽  
Strained Alkenes ◽  
Electron Demand

<p>Strained alkenes and alkynes are the predominant dienophiles used in inverse electron-demand Diels-Alder (IEDDA) reactions, however, their instability, cross-reactivity and accessibility are problematic. Unstrained dienophiles, although physiologically stable and synthetically accessible, react with tetrazines significantly slower relative to strained variants. Here we report the development of potassium arylethynyltrifluoroborates as unstrained dienophiles for ultrafast, chemically triggered IEDDA reactions. By varying the substituents on the tetrazine (e.g. pyridyl- to benzyl-substituents), cycloaddition rates can vary from nearly spontaneous (<i>t</i><sub>1/2</sub>≈ 9 s) to no reaction with the unstrained alkyne-BF3 dienophile. The reported system was applied to protein modification and enabled mutually orthogonal labelling of two distinct proteins.</p>

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