Chemical proteomics interaction

An important factor in all these experiments is the choice of bead used to immobilize the probe. Biochemists have considered cross-linked agarose beads to be exceptionally hydrophilic with a low tendency to bind proteins nonspecifically, and these beads have the further attraction of being commercially available in activated forms (succinimidyl esters, epoxides, and maleimides, for example). However, early trials of bead-based chemical proteomics have shown that many proteins in mammalian cell lysates bind tenaciously to agarose beads. This was unimportant in many studies in which protein-protein interactions were detected by coimmunoprecipitation with immunochemical... 

Wright AT, Cravatt BF (2007) Chemical proteomic probes for profiling cytochrome p450 activities and drug interactions in vivo. Chem Biol 14 1043-1051... 

In general, this approach is often called chemical proteomics, by definition a parallel investigation of the interactions between small molecule libraries and the proteome (proteins that constitute the cell in native or in isolated form in separate experience) at the proteome level. 

Chemical proteomics is a parallel investigation of the interactions between small molecule libraries and their binding proteins at the proteome level. 

Chemical proteomics consists of the classical drug-affinity chromatography and modern high-resolution MS analysis for protein identification [3, 11]. The procedure typically involves immobilization of the compound of interest to a solid support through a spacer arm, and the affinity matrix is then used to purify specific interacting proteins from cellular lysate. The complex proteomic mixture is then proteolytically digested, and the resulting peptides are sequenced... 

Zhang H,Tang X, Munske GR, et al. In vivo identification of the outer membrane protein OmcA-MtrC interaction network in Shewanella oneidensis MR-1 cells using novel hydrophobic chemical cross-linkers. J. Proteome Res. 2008 7 1712-1720. 

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