Effect of thermal stability on protein adsorption to silica using homologous aldo-keto reductases.

ABSTRACT: Gaining more insight into the 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 impact of structural stability on interfacial behavior has been previously investigated by engineering nonwild-type stability mutants. Potential shortcomings of such approaches include only modest changes in thermostability, and the introduction of changes in the topology of the proteins when disulfide bonds are incorporated. Here we employ two members of the aldo-keto reductase superfamily (alcohol dehydrogenase, AdhD and human aldose reductase, hAR) to gain a new perspective on the rol

SUBMITTER: Felsovalyi F 

PROVIDER: S-EPMC3537233 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature