Elucidating mechanisms governing the behavior of proteins at solid/liquid interfaces is particularly relevant in the interaction of high-value biologics with storage and delivery device surfaces, where adsorption-induced conformational changes may dramatically affect biocompatibility. The marked impact of structural stability on interfacial behavior has been investigated by engineering non-wild-type stability mutants by artificially introducing disulfide bonds. A potential shortcoming of such mutants is the inability to decouple the mutation used to enhance stability from its effect on adsorption. We employ two members of the aldo-keto reductase superfamily to gain a new perspective on the role of naturally occurring thermostability on adsorbed protein arrangement and its subsequent impact on desorption. We report that thermostability plays considerably different roles in the distinct kinetic legs of the adsorption-desorption lifecycle. Although structural transitions upon adsorption occur independent of thermostability, the latter plays a major role in determining the reversibility pathway which drives refolding upon desorption.

Assessing the impact of thermal stability on protein adsorption behavior using naturally occurring enzymes of the aldo-keto reductase superfamily

243rd National Meeting (2012)

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