Molecules at Interfaces

Proteins constitute the most widely employed class of biomolecules in surface functionalization. In fact, several biotechnology applications (e.g. implants, biosensors, … ) hinge on a detailed control of protein adsorption. For instance, COVID antigen-testing immunoassays require IgG-proteins to adsorb in bio-active conformations (folded and with the antigen-binding-sites free). This technological interest fueled a vibrant research with the purpose of controlling protein–surface interaction. However, the inherent difficulties of probing events at an atomistic level have severely limited our understanding of this complex process. Powered by new computational architectures (GPUs) we have successfully bridged this gap using all-atom molecular dynamics to simulate how the most abundant plasma proteins adsorb over a plethora of technologically relevant substrates. Naming a few …

I) We showed that antibodies suitably binds to graphene whilst maintaining active sites free for recognition. Our results showed an unprecedentedly high adsorption ratio along functional adsorption configurations – thus significantly improving signal to noise ratio of antibodies based biosensors [x].

II) We showed that commonly used implicit solvent methods fail to reproduce the adsorption of the most abundant plasma proteins (as corroborated by experiments). Beyond a methodological milestone, this work also unveiled a pivotal role entropic forces in controlling the adsorption.[x]