scholarly journals Anti-EGFR Affibodies with Site-Specific Photo-Cross-Linker Incorporation Show Both Directed Target-Specific Photoconjugation and Increased Retention in Tumors

2018 ◽  
Vol 140 (37) ◽  
pp. 11820-11828 ◽  
Author(s):  
Michael Brasino ◽  
Shambojit Roy ◽  
Annette H. Erbse ◽  
Liangcan He ◽  
Chenchen Mao ◽  
...  
Keyword(s):  
Site Specific ◽  
Cross Linker ◽  
Increased Retention

Site-Specific Incorporation of Photo-Cross-Linker and Bioorthogonal Amino Acids into Enteric Bacterial Pathogens

2011 ◽  
Vol 133 (50) ◽  
pp. 20581-20587 ◽  
Author(s):  
Shixian Lin ◽  
Zhenrun Zhang ◽  
Hao Xu ◽  
Lin Li ◽  
She Chen ◽  
...  
Keyword(s):  
Amino Acids ◽  
Bacterial Pathogens ◽  
Site Specific ◽  
Cross Linker

Genetically encoding phenyl azide chemistry: new uses and ideas for classical biochemistry

2013 ◽  
Vol 41 (5) ◽  
pp. 1177-1182 ◽  
Author(s):  
Samuel Reddington ◽  
Peter Watson ◽  
Pierre Rizkallah ◽  
Eric Tippmann ◽  
D. Dafydd Jones
Keyword(s):  
Protein Function ◽  
Unnatural Amino Acid ◽  
Amino Acid Incorporation ◽  
Phenyl Azide ◽  
Site Specific ◽  
Acid Incorporation ◽  
Cross Linker ◽  
Natural Amino Acids ◽  
Modify Protein

Introducing new physicochemical properties into proteins through genetically encoded Uaa (unnatural amino acid) incorporation can lead to the generation of proteins with novel properties not normally accessible with the 20 natural amino acids. Phenyl azide chemistry represents one such useful addition to the protein repertoire. Classically used in biochemistry as a non-specific photochemical protein cross-linker, genetically encoding phenyl azide chemistry at selected residues provides more powerful routes to post-translationally modify protein function in situ. The two main routes are modulation by light (optogenetics) and site-specific bio-orthogonal modification (bioconjugation) via Click chemistry. In the present article, we discuss both approaches and their influence on protein function.

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.

The challenge of detecting modifications on proteins

2020 ◽  
Vol 64 (1) ◽  
pp. 135-153 ◽  
Author(s):  
Lauren Elizabeth Smith ◽  
Adelina Rogowska-Wrzesinska
Keyword(s):  
Mass Spectrometry ◽  
Protein Function ◽  
Chemical Properties ◽  
Lysine Acetylation ◽  
Mass Determination ◽  
Post Translational Modifications ◽  
Site Specific ◽  
The Common

Abstract Post-translational modifications (PTMs) are integral to the regulation of protein function, characterising their role in this process is vital to understanding how cells work in both healthy and diseased states. Mass spectrometry (MS) facilitates the mass determination and sequencing of peptides, and thereby also the detection of site-specific PTMs. However, numerous challenges in this field continue to persist. The diverse chemical properties, low abundance, labile nature and instability of many PTMs, in combination with the more practical issues of compatibility with MS and bioinformatics challenges, contribute to the arduous nature of their analysis. In this review, we present an overview of the established MS-based approaches for analysing PTMs and the common complications associated with their investigation, including examples of specific challenges focusing on phosphorylation, lysine acetylation and redox modifications.

MEMORY EFFECTS IN THE FRAGMENTATION OF MOLECULES FOLLOWING SITE-SPECIFIC CORE EXCITATION

1987 ◽  
Vol 48 (C9) ◽  
pp. C9-741-C9-744 ◽  
Author(s):  
W. HABENICHT ◽  
L. A. CHEWTER ◽  
M. SANDER ◽  
K. MÜLLER-DETHLEFS ◽  
E. W. SCHLAG
Keyword(s):  
Memory Effects ◽  
Core Excitation ◽  
Site Specific
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