Strong structural and electronic binding of bovine serum albumin to ZnO via specific amino acid residues and zinc atoms

0561891 - FZÚ 2023 RIV DE eng J - Článek v odborném periodiku
Hematian, H. - Ukraintsev, Egor - Rezek, B.
Strong structural and electronic binding of bovine serum albumin to ZnO via specific amino acid residues and zinc atoms.
ChemPhysChem. Roč. 23, č. 2 (2022), s. 25-33. ISSN 1439-4235. E-ISSN 1439-7641
Grant CEP: GA ČR GC19-02858J
Výzkumná infrastruktura: CzechNanoLab - 90110
Institucionální podpora: RVO:68378271
Klíčová slova: bovine serum albumin * ZnO * atomic force microscopy * nanoshaving * density-functional tight-binding
Obor OECD: Fluids and plasma physics (including surface physics)
Impakt faktor: 2.9, rok: 2022
Způsob publikování: Omezený přístup
https://doi.org/10.1002/cphc.202100639

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 on the structural, optical, and electronic properties of albumin-ZnO complexes. Yet there are still large gaps in the understanding of these biological interfaces. Herein we comprehensively elucidate the interactions at such interfaces by using atomic force microscopy and nanoshaving experiments to determine roughness, thickness, and adhesion properties of BSA layers adsorbed on the most typical polar and non-polar ZnO single-crystal facets. These experiments are corroborated by force field (FF) and DFTB calculations on 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.

Trvalý link: https://hdl.handle.net/11104/0334322