  Engineered biomedical nanoparticles (NP) administered via intravenous routes
are prone to associate to serum proteins. The protein corona can mask the NP
surface functionalization and hamper the delivery of the NP to its biological
target. The design of corona-free NPs relies on our understanding of the
chemical-physical features of the NP surface driving the interaction with serum
proteins. Here we address, by computational means, the interaction between
human serum albumin (HSA) and a prototypical monolayer-protected Au
nanoparticle. We show that both the chemical composition (charge,
hydrophobicity) and the conformational preferences of the ligands decorating
the NP surface affect the NP propensity to bind HSA.
