Understanding of nonspecific protein adsorption mechanisms at solid-liquid interfaces is critical to rational design of surfaces for biomedical and industrial applications, such as medical devices, drug delivery carriers, marine coating, and biosensors. For blood-contacting medical devices, for example, contact with blood results in rapid nonspecific protein adsorption. This protein layer may initiate blood clotting by promoting platelet adhesion, activation, and aggregation. Therefore, materials are often engineered to enhance resistance to nonspecific protein adsorption through surface modification. Optimizing the design of blood compatible surfaces requires a detailed understanding of protein-surface interactions.<br/>Protein interaction with solid interfaces is a result of transport, adsorption, desorption, and reaction processes. Individual protein surface interactions can result in reversible or irreversible binding, and some proteins may also undergo conformational changes after adsorption. Constructing a detailed model of protein-surface interactions requires that these phenomena be observable at the single-molecule level.<br/>We have studied the dynamics of protein adsorption on synthetic surfaces including polyelectrolyte multilayers, glycocalyx-like surface coatings, and PEG surfaces. We have used single-molecule tracking to measure a large number of single protein trajectories (&gt;10<sup>4</sup> in each experiment) to explicitly visualize the processes of adsorption and desorption of albumin and fibrinogen on these model surfaces. These direct experimental observations inform a mathematical model that describes protein adsorption and desorption and possible denaturation. This detailed characterization of protein-surface interactions can be used to design improved glycocalyx mimetic surfaces for blood-contacting biomaterials.

Designing biomimetic interfaces for blood-contacting biomaterials: New insights from single-molecule microscopy

2019 Spring National Meeting

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