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.
protein labeling 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.
Peptide and protein thioester 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.
Getting a chemical handle on
protein post-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.
Synthesis and application of a new cleavable linker for “click”-based
“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.
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.
Proteasome selectivity towards Michael acceptor containing
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.
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.
neoglycoprotein assembly 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.
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.
Practical synthesis of maleimides and
coumarin-linked probes for protein and antibody labellingvia reduction 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.
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.