Estimating and leveraging protein diffusion on ion-exchange resin surfaces.

ABSTRACT: Protein mobility at solid-liquid interfaces can affect the performance of applications such as bioseparations and biosensors by facilitating reorganization of adsorbed protein, accelerating molecular recognition, and informing the fundamentals of adsorption. In the case of ion-exchange chromatographic beads with small, tortuous pores, where the existence of surface diffusion is often not recognized, slow mass transfer can result in lower resin capacity utilization. We demonstrate that accounting for and exploiting protein surface diffusion can alleviate the mass-transfer limitations on multiple significant length scales. Although the surface diffusivity has previously been shown to correlate with ionic strength (IS) and binding affinity, we show that the dependence is solely on the binding

SUBMITTER: Khanal O 

PROVIDER: S-EPMC7132105 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature