Insights into graphene oxide interaction with human serum albumin in isolated state and in blood plasma

The interactions of graphene oxide (GO), a 2-dimensional nanomaterial with hydrophilic edges, hydrophobic basal plane and large flat surfaces, with biological macromolecules, are of key importance for the development of novel nanomaterials for biomedical applications. To gain more insight into the interaction of GO flakes with human serum albumin (HSA), we examined GO binding to HSA in its isolated state and in blood plasma. Calorimetric data reveal that GO strongly stabilizes free isolated HSA against a thermal challenge at low ionic strength, indicating strong binding interactions, confirmed by the drop in zeta-potential of the HSA/GO assemblies compared to bare GO flakes. However, calorimetry also revealed that the HSA-GO molecular interaction is hampered in blood plasma, the ionic strength being particularly important for the interactions. Molecular modelling calculations are in full concert with these experimental findings, indicating a considerably higher binding affinity for HSA to GO in its partially unfolded state, characteristic to low-ionic-strength environment, than for the native protein conformation, observed under physiological conditions. Therefore, for the first time we demonstrate an impeded interaction between HSA and GO nanoflakes in blood plasma, and suggest that the protein is protected from the plausible toxic effects of GO under native conditions. (C) 2021 Elsevier B.V. All rights reserved.

Automated summary

The study reveals that the interaction between graphene oxide and human serum albumin is strong in the isolated state but limited in blood plasma, with ionic strength playing a crucial role in these interactions. Molecular modeling calculations support these findings, showing a higher binding affinity in a low-ionic-strength environment compared to physiological conditions.