Metallic Engineered Nanomaterials and Ocular Toxicity: A Current Perspective.

The ocular surface, comprised of the transparent cornea, conjunctiva, and protective tear film, forms a protective barrier defending deeper structures of the eye from particulate matter and mechanical trauma. This barrier is routinely exposed to a multitude of naturally occurring and engineered nanomaterials (ENM). Metallic ENMs are particularly ubiquitous in commercial products with a high risk of ocular exposure, such as cosmetics and sunscreens. Additionally, there are several therapeutic uses for metallic ENMs owing to their attractive magnetic, antimicrobial, and functionalization properties. The increasing commercial and therapeutic applications of metallic ENMs come with a high risk of ocular exposure with poorly understood consequences to the health of the eye. While the toxicity of metallic ENMs exposure has been rigorously studied in other tissues and organs, further studies are necessary to understand the potential for adverse effects and inform product usage for individuals whose ocular health may be compromised by injury, disease, or surgical intervention. This review provides an update of current literature on the ocular toxicity of metallic ENMs in vitro and in vivo, as well as the risks and benefits of therapeutic applications of metallic ENMs in ophthalmology.

Voltammetric study of conductive planar assemblies of Geobacter nanowire pilins unmasks their ability to bind and mineralize divalent cobalt.

Geobacter bacteria assemble a helical peptide of the Type IVa pilin subclass as conductive pili decorated with metal binding and reduction sites. We used recombinant techniques to synthesize thiolated pilin derivatives and self-assembled them on gold electrodes as a monolayer that concentrated the metal traps at the liquid interface. Cyclic and step potential voltammetry demonstrated the conductivity of the pilin films and their ability to bind and reductively precipitate divalent cobalt (Co2+) in a diffusion-controlled reaction characterized by fast binding kinetics, efficient charge transfer, and three-dimensional nanoparticle growth at discreet sites. Furthermore, cobalt oxidation at the pilin film was slower than on bare gold, consistent with a peptide optimized for metal immobilization. These properties make recombinant pilins attractive building blocks for the synthesis of novel biomaterials for the immobilization of toxic cationic metals that, like Co2+, are sparingly soluble and, thus, less mobile and bioavailable as reduced species.

Electronic characterization of Geobacter sulfurreducens pilins in self-assembled monolayers unmasks tunnelling and hopping conduction pathways.

The metal-reducing bacterium Geobacter sulfurreducens produces protein nanowires (pili) for fast discharge of respiratory electrons to extracellular electron acceptors such as iron oxides and uranium. Charge transport along the pili requires aromatic residues, which cluster once the peptide subunits (pilins) assemble keeping inter-aromic distances and geometries optimal for multistep hopping. The presence of intramolecular aromatic contacts and the predominantly α-helical conformation of the pilins has been proposed to contribute to charge transport and rectification. To test this, we self-assembled recombinant, thiolated pilins as a monolayer on gold electrodes and demonstrated their conductivity by conductive probe atomic force microscopy. The studies unmasked a crossover from exponential to weak distance dependence of conductivity and shifts in the mechanical properties of the film that are consistent with a transition from interchain tunneling in the upper, aromatic-free regions of the helices to intramolecular hopping via aromatic residues at the amino terminus. Furthermore, the mechanistic stratification effectively "doped" the pilins at the amino terminus, favoring electron flow in the direction opposite to the helix dipole. However, the effect of aromatic dopants on rectification is voltage-dependent and observed only at the low (100 mV) voltages that operate in biological systems. The results thus provide evidence for a peptide environment optimized for electron transfer at biological voltages and in the direction needed for the respiration of external electron acceptors. The implications of these results for the development of hybrid devices that harness the natural abilities of the pilins to bind and reduce metals are discussed.