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Themed collection Protein Labelling and Chemical Proteomics

11 items
Perspective

The use of click chemistry in the emerging field of catalomics

This perspective surveys the significant contributions of click chemistry in catalomics (a sub-area in chemical proteomics), with special emphasis on activity-based protein profiling (ABPP), posttranslational modifications (PTMs) and enzyme inhibitor developments.

Graphical abstract: The use of click chemistry in the emerging field of catalomics
From the themed collection: Protein Labelling and Chemical Proteomics
Perspective

Site specific proteinlabeling by enzymatic posttranslational modification

This perspective reviews the use of protein posttranslational modification enzymes to label proteins with chemical probes of diverse structures and functionalities.

Graphical abstract: Site specific protein labeling by enzymatic posttranslational modification
From the themed collection: Protein Labelling and Chemical Proteomics
Emerging Area

Peptide and proteinthioester synthesisvia N→S acyl transfer

Peptide thioesters are playing an increasingly prominent role in the chemical toolbox for protein assembly and modification through Native Chemical Ligation (NCL). In this article we highlight recent developments in thioester production through selective disruption of amide bonds.

Graphical abstract: Peptide and protein thioester synthesis via N→S acyl transfer
From the themed collection: Protein Labelling and Chemical Proteomics
Emerging Area

Getting a chemical handle on proteinpost-translational modification

Chemical proteomics is a powerful technology for the study of post- and co-translational modification of proteins. Here, we review techniques that combine protein-modifying enzymes with bioorthogonal chemoselective elaboration to enable new advances in our understanding of protein modification.

Graphical abstract: Getting a chemical handle on protein post-translational modification
From the themed collection: Protein Labelling and Chemical Proteomics
Communication

Synthesis and application of a new cleavable linker for “click”-based affinity chromatography

“Click” coupling of a ligand to an azo-functionalised linker allows affinity capture and separation of proteins from a complex mixture (such as fetal bovine serum) and mild release with sodium dithionite.

Graphical abstract: Synthesis and application of a new cleavable linker for “click”-based affinity chromatography
From the themed collection: Protein Labelling and Chemical Proteomics
Communication

Clickable fluorescent dyes for multimodal bioorthogonal imaging

Clickable 2-dicyanomethylene-3-cyano-2,5-dihydrofuran fluorescent dyes presented here enable multimodal bioorthogonal imaging of azide- and alkyne-modified proteins in vitro and in cells.

Graphical abstract: Clickable fluorescent dyes for multimodal bioorthogonal imaging
From the themed collection: Protein Labelling and Chemical Proteomics
Paper

Proteasome selectivity towards Michael acceptor containing oligopeptide-based inhibitors

Ten Michael acceptors combined with three peptide elements yields 30 potential proteasome inhibitors. These compounds were assessed for their proteasome inhibitory capacities. Cellular targets of two compounds were determined by a two step labeling, affinity purification and LC/MS2 approach.

Graphical abstract: Proteasome selectivity towards Michael acceptor containing oligopeptide-based inhibitors
From the themed collection: Protein Labelling and Chemical Proteomics
Paper

Fluorescence quenched quinone methide based activity probes – a cautionary tale

A carbamate linked quenching group coupled with a pro-quinone methide reactive core provides an effective tool for studying enzyme function without problems associated with background fluorescence. However protein labelling observations should be treated with caution.

Graphical abstract: Fluorescence quenched quinone methide based activity probes – a cautionary tale
From the themed collection: Protein Labelling and Chemical Proteomics
Paper

Exploring neoglycoproteinassembly through native chemical ligation using neoglycopeptide thioesters prepared via N→S acyl transfer

Sugars and simplified oligosaccharide “mimics” can be joined with protein fragments at pre-defined sites and assembled into potential neoglycoprotein therapeutics using native chemical ligation.

Graphical abstract: Exploring neoglycoprotein assembly through native chemical ligation using neoglycopeptide thioesters prepared via N→S acyl transfer
From the themed collection: Protein Labelling and Chemical Proteomics
Paper

Clickable fluorophores for biological labeling—with or without copper

The synthesis and applications of a set of new clickable fluorophores covering the whole visible spectrum reaching the near infra-red regime is presented herein.

Graphical abstract: Clickable fluorophores for biological labeling—with or without copper
From the themed collection: Protein Labelling and Chemical Proteomics
Paper

Practical synthesis of maleimides and coumarin-linked probes for protein and antibodylabellingviareduction of native disulfides

Reduction of disulfides within antibodies and cysteine-based fluorescent tagging with a readily made, water-soluble maleimide reagent allows for a convenient way to sort cells and label proteins.

Graphical abstract: Practical synthesis of maleimides and coumarin-linked probes for protein and antibody labelling via reduction of native disulfides
From the themed collection: Protein Labelling and Chemical Proteomics
11 items

About this collection

Organic & Biomolecular Chemistry's web theme issue on Protein Labelling and Chemical Proteomics is now published. The articles and an introduction from the Guest Editors can be viewed below.

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