Tobias Baumgart and Ivan J. Dmochowski
Protein assembly at the air-water interface (AWI) occurs naturally in many biological processes, and provides a method for creating ordered biomaterials. However, the factors that control protein self-assembly at the AWI are generally not well understood. Here, we describe the behavior of a model protein, human serum albumin minimally labeled with Texas Red dye (HSA-TR), using a new confocal microscopy technique (Figure 1). Albumin was observed to form well-ordered, mesoscale monolayer structures at the AWI (Figure 2), which depended on protein concentration, ionic strength, redox state and surfactant. We are investigating thermodynamic and kinetic details of assembly.