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The use of bionanoparticles at interfaces has a long history, ranging from beer brewing to the material science of natural biological structures. In beer, the proteins reside at the gas/liquid interface, which provides a nice foam that is appreciated by many. Also in the case of whipped cream, milk foams and whipped egg whites, the airy mixture is stabilized due to the high affinity of protein structures at polar/apolar interfaces.1  In natural systems, proteins are also found at interfaces and often at solid/liquid interfaces, as is seen in the build-up of bone and teeth structures, but proteins also play important roles at lipid bilayer interfaces.2  Because of these large variations in the function of proteins at interfaces, more emphasis is placed on understanding how proteins behave at interfaces with respect to adsorption kinetics/thermodynamics, structural changes, packing and retention of primary function, e.g. catalysis. These understandings provide the foundation for biocompatible materials, which are not only interesting for industry to improve food quality, functionalize textiles3  and to design micro-reactors, but also serve as a platform for biohybrid materials relevant for (bio-)medical applications, e.g. drug delivery and materials that can be used in tissue engineering.2,4–8 

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