The dominant cost of manufacturing biologically-based pharmaceuticals is associated with purification, possibly caused by a lack in the molecular-scale understanding of the dynamics of biological macromolecules in the charged and crowded environment of the functionalized adsorbent surfaces used in separations.  Heterogeneous binding dynamics in such a synthetic system can be obscured by ensemble characterization techniques.  We have developed methods that allow us to use single molecule fluorescence microscopy to study the dynamics of the protein alpha-lactalbumin at a unique, clustered-charge anion-exchange chromatographic adsorbent surface, as it has been hypothesized that traditional ion-exchange protein separations are dominated by adsorption at accidental, or stochastic, clustering of charges on the adsorbent surface. This presentation addresses method development and preliminary results in understanding the ion-exchange process at single protein scales, and addresses our efforts to characterize and distinguish between free diffusion, hindered diffusion, and adsorption/desorption events.

Protein dynamics at a heterogeneous clustered-charge ion-exchange adsorbent interface

244th National Meeting (2012)

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