Molecular mechanisms in oxide nanoparticle interactions with proteins

Nanoparticles of potentially biocompatible sand minerals, metal oxides, were recently proved to form complexes with protein molecules through strong and specific binding with ordered alpha-helix fragments.

This complex formation was observed for such important classes of biomolecules as blood proteins, responsible for clotting and tissue regeneration, and for viral proteins arresting the cell response.

In the proposed study, we aim to bring understanding for the mechanisms of nanoparticle-protein interactions at molecular level.

As we recently demonstrated, crucial insights into bonding and reactivity of nanoparticles can be obtained using as models individual polyoxometallate (POM) species – smallest oxide nanoparticles – just over 1 nm in size.

We plan to construct on purpose POM imitating the surface of iron, titanium, zirconium, cerium, and aluminium oxide nanoparticles and investigate the structure and reactivity of their complexes with peptide fragments resembling the identified potential binding sites, and with selected key classes of proteins, applying X-ray diffraction, X-ray spectroscopy, and solution and solid-state nuclear magnetic resonance (NMR) spectroscopy.

Data on bonding modes and parameters will be able to contribute to development of predictive computational tools based on molecular dynamics approaches.

The overall goal will be to create basis for potential control over protein binding and aggregation for further verification via in vitro experiments.