Detailed insights into the mechanisms governing the behavior of proteins at solid/liquid interfaces are particularly relevant in prefilled drug-delivery systems, where adsorption-induced conformational changes may dramatically affect biocompatibility when high-value biologics contact device surfaces. Although we have the reasonably sound understanding that adsorption generally leads to the perturbation of secondary structure, relatively little is known about how history-dependence of surface-related events affect subsequent desorption. With the goal of elucidating desorption predictability for specific systems, we evaluate structural transitions and kinetic parameters along the adsorption-desorption lifecycle of several proteins on nanoparticle surfaces of varying hydrophobicity, as a function of surface coverage. Screening proteins based on stability and charge difference with the surface enables us to rank the role of electrostatics and intrinsic stability in reversibility of adsorption and pathways of desorption. We find that charge difference plays a determining role in whether Langmuiran parameters can be used to predict desorption behavior.

What determines protein desorption behavior?

243rd National Meeting (2012)

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