Proteins constitute the largest and most widely employed class of biomolecules in surface functionalization. There is a wide range of applications in biotechnology that rely on protein adsorption such as biocompatible interfaces, biosensorifis, and interfaces for tissue engineering and regenerative medicine. One common requirement in these applications is that the protein must remain bioactive upon deposition. Protein adsorption also represents an interesting and important fundamental problem because it is the result of a delicate interplay among protein–surface interactions, hydration forces, and the protein’s ability to change its conformation.

Fueled by its fundamental and technological interest, much effort has been devoted in understanding and controlling protein–surface interaction from an experimental point of view. Yet, the inherent difficulties to probe events at an atomistic level has limited our understanding of this complex process and as a result most devices dependent on protein-surface interactions are developed on a trial error approach. To bridge this gap and enable a knowledge based approach, over the past years we employed all-atom molecular dynamics simulations to study the adsorption of the most abundant plasma proteins to inorganic surfaces.

Our works have unraveled a wide range of surprising results, to name a few: