Chemical Proteomics

Chemical proteomics makes use of synthetic organic chemistry. A central component of this field is the design of specific protein-modifying reagents that can be used for functional studies of distinct enzyme families within a complex proteome. These chemical probes are designed to covalently modify a target enzyme in such a way that it can be subsequently identified and/or purified.

In their most basic form, chemical probes consist of the following 3 distinct functional elements:

• reactive group; for covalent attachment to the enzyme. This reactive group must be both reactive towards a specific residue on a protein and inert towards other reactive species within the cell or cell extract.

• linker group; can serve many purposes. Its primary one is to provide enough space between the reactive group and the tag to prevent steric hindrance that could block access of the reactive group or accessibility of the tag for the purpose of purification.

• tag; for identification and purification of modified enzymes

Activity-Based Enzyme Modifiers (ABPs):  are a method of visualizing enzyme activities using small molecule probes that covalently attach to an enzyme target using chemical interactions that are specific for the target enzyme(s). The chemical reagent has the ability to recognize a conserved catalytic/functional/structural motif in a family of active proteins, to react with the target proteins in a covalent manner based on its conserved motif and to quantify the amount of each active protein.

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