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Small-Molecule Affinity-Based Matrices for Rapid Protein Purification

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Affinity chromatography, the method of purifying target proteins from complex mixtures using immobilized affinity ligands on chromatographic supports, is perhaps the most common of all affinity techniques ( 13 ). Many affinity chromatography systems are comprised of activated supports requiring direct ligand-coupling procedures that can be complex, time-consuming, and result in low- or variable-capacity columns supporting immobilized ligands with poor activity ( 25 ). We describe here a method that improves this technology by using a small-molecule based chemical affinity technology ( 6 ) to quickly and easily prepare high-capacity affinity columns supporting functionally active capture ligands for purifying proteins from crude mixtures ( 7 , 8 ). This innovation is based on the specific interaction between two, non-biological, small molecules, phenyl-diboronic acid (PDBA) and salicylhydroxamic acid (SHA) ( see Fig. 1 ).
Fig. 1.  PDBA:SHA Chemical Affinity System. The reaction of phenyldiboronic acid (PDBA) with salicylhydroxamic acid (SHA). The SHA is covalently anchored to the surface of crosslinked agarose chromatography media and a PDBA derivative is conjugated to a protein of choice.

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