Bovine insulin has long been known to self-assemble in vitro into amyloid fibrils. We have observed a further higher-order selfassociation of the protein into spherical structures, with diameters typically around 50 m but ranging from 10 to 150 m. In a polarizing light microscope, these structures exhibit a ''Maltesecross'' extinction pattern typical of spherulites. Spherical structures of a similar size distribution can be observed in the environmental scanning electron microscope, which also reveals the presence of significant amounts of water in the structures. The spherulites contain a large quantity of well defined amyloid fibrils, suggesting that they are formed at least in part as a consequence of the self-assembly of preformed fibrils. Similar structures also have been observed in the tissues of patients suffering from amyloid disorders. The ability of amyloid fibrils to form such higher-order assemblies supports the hypothesis that they represent a generic form of polypeptide structure with properties that are analogous to those of classical synthetic polymers.

We have measured normal and lateral interactions across a range of different liquids between mica surfaces using a surface force balance (SFB). The mica surfaces were prepared either by melt cutting using Pt wire and standard procedures in our laboratories or by tearing sheets (that had not been exposed to Pt) off from a freshly cleaved sheet of mica. AFM micrographs revealed the substantial absence of Pt nanoparticles on the melt cut and torn-off mica surfaces. Normal-force versus surface-separation (D) profiles and shear force versus D measurements for purified water (no added salt), for concentrated aqueous NaCl solutions, and for cyclohexane revealed that in all cases the behavior of the highly confined liquids between melt-cut and between torn-off mica sheets was identical within experimental scatter. These results demonstrate directly that interactions measured between melt-cut mica surfaces as routinely prepared using established procedures in our laboratories and in other laboratories are free of the effect of any Pt contamination.

The growing use of silver nanoparticles (AgNPs) in consumer products has raised concerns about their potential impact on the environment and human health. Whether AgNPs dissolve and release Ag+ ions, or coarsen to form large aggregates, is critical in determining their potential toxicity. In this work, the stability of AgNPs in dipalmitoylphosphatidylcholine (DPPC), the major component of pulmonary surfactant, was investigated as a function of pH. Spherical, citrate-capped AgNPs with average diameters of 14 ± 1.6 nm (n=200) were prepared by a chemical bath reduction. The kinetics of Ag+ ion release was strongly pH-dependent. After 14 days of incubation in sodium perchlorate (NaClO4) or perchloric acid (HClO4) solutions, the total fraction of AgNPs dissolved varied from ~10 % at pH 3, to ~2 % at pH 5, with negligible dissolution at pH 7. A decrease in pH from 7 to 3 also promoted particle aggregation and coarsening. DPPC (100 mg.L−1) delayed the release of Ag+ ions, but did not significantly alter the total amount of Ag+ released after two weeks. In addition, DPPC improved the dispersion of the AgNPs and inhibited aggregation and coarsening. TEM images revealed that the AgNPs were coated with a DPPC layer serving as a semi-permeable layer. Hence, lung lining fluid, particularly DPPC, can modify the aggregation state and kinetics of Ag+ ion release of inhaled AgNPs in the lung. These observations have important implications for predicting the potential reactivity of AgNPs in the lung and the environment.