The ability to control the specific adsorption and packing behaviors of biomedically important proteins by effectively guiding their preferred surface adsorption configuration and packing orientation on polymeric surfaces may have utility in many applications such as biomaterials, medical implants, and tissue engineering. We examine the distinct adhesion configurations of fibrinogen (Fg) proteins and the different organization behaviors between single Fg molecules that are mediated by the changes in the periodicity and alignment of chemically alternating nanodomains in the thin films of polystyrene-block-polymethylmethacrylate (PS-b-PMMA) block copolymer (BCP). <i>Via</i> direct visualization by high resolution imaging, the distinct adsorption and packing configurations of both isolated and interacting Fg molecules are determined as a function of the BCP template-specific nanodomain periodicity, domain alignment (random <i>versus</i> fully aligned), and protein concentration. During surface packing, the orientation of the protein backbone is largely governed by the periodicity and alignment of the underlying PS-b-PMMA nanodomains whose specific direction is explicitly resolved relative to the polymeric nanodomain axis. We have successfully created fully Fg-decorated BCP constructs analogous to two-dimensional Fg crystals in which aligned protein molecules are arranged either side-on or end-on, depending on the BCP template. Our results demonstrate that the geometry and orientation of the protein can be effectively guided during Fg self-assembly by controlling the physical dimensions and orientations of the underlying BCP templates.

Surface assembly and packing preferences of fibrinogen mediated by the periodicity and alignment of block copolymer nanodomains

253rd National Meeting (2017)

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