Facet-Specific Assembly of Proteins on SrTiO3 Polyhedral Nanocrystals

Abstract

Precisely controlling the protein-nanomaterial interactions at selective sites is crucial in engineering biomolecule composite architectures with tailored nanostructures and functions for a variety of biomedical applications. This strategy, however, is only beginning to be explored. Here, we demonstrate the facet-specific assembly of proteins, such as albumin, immunoglobulin and protamine, on {100} facets of SrTiO3 polyhedral nanocrystals, while none on {110} facets. Molecular dynamics simulations indicate the immobile surface hydration layer might play a barrier role to effectively prevent proteins adsorption on specific {110} facets. This work thus provides new insights into the fundamentally understanding of protein-nanomaterial interactions, and open a novel, general and facile route to control the selective adsorption of various proteins on various nanocrystals.

A cuboidal B2 nanoprecipitation-enhanced body-centered-cubic alloy Al0.7CoCrFe2Ni with prominent tensile properties

“…A solute showing a negative H tends to occupy the cluster center and then the glue site, and that showing a weak H tends to take the glue site. Such a cluster-based formulism has been validated in a variety of FCC and BCC alloys [18,19], confirming that widely-used alloys generally satisfy a limited number of specific composition formulas. Taking the BCC solid solutions for instance, the cluster is a rhombi-dodecahedron with a coordination number of 14 (CN14), and the cluster formula is expressed with the [rhombi-dodecahedron](glue atoms) x .…”

“…Pronounced Al-TM nearest-neighbor atomic pairs have been unveiled in an Al 1.3 CoCrCuFeNi multi-principal element alloy by neutron diffraction [17]. A new structural approach, the cluster-plus-glue-atom model [18], was recently introduced to address the structural modeling of solid solutions. In this model, any chemical short-range order is idealized into a local nearest-neighbor coordination polyhedral cluster and the sites in-between the clusters are filled with glue atoms, which could be expressed with a composition formula of [cluster](glue atoms) x (x is the glue atom number for matching one cluster).…”

Peering into the Formation of Template-Free Hierarchical Flowerlike Nanostructures of SrTiO3

“…The {110} surface had its strontium atoms removed for stabilization, as suggested before. 58 Slabs, of about 45 × 45 Å 2 (periodic along the x and y directions) and a thickness along z (perpendicular to the surface) that is enough for the bulk density far from the surface to reach a constant value, were put in contact with vinylpyrrolidone trimers with density corresponding to its bulk under the relevant conditions, at 433 K (synthesis temperature of 160 °C for solvothermal reaction) for 10 ns (long enough for system equilibration), as performed in similar works. 59 The Nosé–Hoover thermostat was used for temperature control.…”

Nanocrystal facet modulation to enhance transferrin binding and cellular delivery

“…For example, thermal hysteresis proteins, a group of serum proteins commonly present in organisms living in cold environments, bind to specific faces of ice crystals to enable their antifreeze activity 13,14 . Recent theoretical studies point to the possibility of facet-dependent selective binding of amino acids, peptides, proteins, and DNA to crystal surfaces containing metals [15][16][17][18][19] . Here, we experimentally prove the concept that facet engineering may be utilized to tune the nanocrystal-biomolecule association for refining biological applications of crystalline nanomaterials.…”