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Activity-based probes can be used for monitoring enzyme activity based on their covalent reactions with active-site residues. A quenched activity-based probe has now been developed that becomes fluorescent only after labeling active proteases. The specificity of the fluorescent signal and cell permeability of the small molecule make this probe effective for monitoring protease activity in living cells.
The growth of research at the chemistry-biology interface provides a unique opportunity to inspire undergraduate students to pursue careers in science and to educate science and nonscience students broadly in both chemical and biological sciences.
Chemical genomic approaches offer an alternative to traditional high-throughput screening for drug discovery and provide an emerging approach to probing cellular biology. The 58th Ernst Schering Foundation Workshop on “Chemical Genomics: Small Molecule Probes to Study Cellular Function,” held April 6–8, 2005, in Berlin, Germany, captured recent chemical genomics advances and highlighted the power of a tight integration of chemistry and biology.
Chemical biologists studying natural-product pathways encoded in genomes have unearthed new chemistry and insights into the evolution of biologically active metabolites.
Protein nitrosation is an important signaling mechanism in vivo; however, mechanisms for selective nitric oxide modification of cysteines have not been described. Thioredoxin is now shown to rapidly and site-specifically catalyze S-nitrosation of an active site cysteine of caspase-3.
The identification of promising lead compounds from high-throughput screens is still a very complex problem. A new high-throughput assay for identifying aggregation-based false positives could help.
In the competition for control of iron between Mycobacterium tuberculosis and host cells, very little is understood about how these bacteria use small-molecule siderophores to obtain iron. A mechanism is now shown for intracellular iron acquisition by mycobacterial lipophilic siderophores.