| dc.description.abstract |
The ‘capture’ of proteins by small molecules via irreversible cross-linking mediated by photo-irradiation is of interest in the field of proteomics (for reviews see ref. 1). The technique has the potential for profiling protein-binding by small molecules, an objective of importance both for basic cell biology and in pharmaceutical science. Capture compounds, or photoaffinity probes, are typically endowed with three functions comprising (i) a selectivity function, such as an enzyme inhibitor, (ii) a photo-cross linking group (capture function) and (iii) a sorting group to enable separation of the captured protein from biological mixtures, such as biotin or an alkyne for subsequent modification. The captured protein(s) can be isolated using streptavidin beads and identified by mass spectrometry or Western blotting (for examples see ref. 2) |
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