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Strong Structural and Electronic Binding of Bovine Serum Albumin to ZnO via Specific Amino Acid Residues and Zinc Atoms.

ZnO biointerfaces with serum albumin have attracted noticeable attention due to the increasing interest in developing ZnO-based materials for biomedical applications. ZnO surface morphology and chemistry are expected to play a critical role in the structural, optical and electronic properties of albumin-ZnO complexes. Yet there are still large gaps in understanding these biological interfaces. Here we comprehensively elucidate interactions at such interfaces by using atomic force microscopy and nanoshaving experiments to determine roughness, thickness, and adhesion properties of the BSA layers adsorbed on the most typical polar and non-polar ZnO single-crystal facets. These experiments are corroborated by the force field (FF) and density-functional tight-binding (DFTB) calculations of ZnO-BSA interfaces. We show that BSA adsorbs on all the studied ZnO surfaces while interactions of BSA with ZnO are found to be considerably affected by the atomic surface structure of ZnO. BSA layers on the (0001)  surface have the highest roughness and thickness, hinting at a specific upright BSA arrangement. BSA layers on (1010)  surface have the strongest binding, which is well correlated with DFTB simulations showing atomic rearrangement and bonding between specific amino acids (AAs) and ZnO. Besides the structural properties, the ZnO interaction with these AAs controls also charge transfer and HOMO-LUMO energy positions in the BSA-ZnO complexes.