This article describes a systematic study of the nucleation and growth of Ag (and Au) on Pd nanocrystal seeds. By carefully controlling the reaction kinetics, the newly formed Ag atoms could be directed to selectively nucleate and then epitaxially grow on a specific number (ranging from one to six) of the six faces on a cubic Pd seed, leading to the formation of bimetallic nanocrystals with a variety of different structures. In addition to changing the injection rate of precursor, we also systematically investigated other reaction parameters including the capping agent, reductant, and reaction temperature. Our results suggest that the site-selective growth of Ag on cubic Pd seeds could be readily realized by optimizing these reaction parameters. On the basis of the positions of Pd seeds inside the bimetallic nanocrystals as revealed by TEM imaging and elemental mapping, we could identify the exact growth pathways and achieve a clear and thorough understanding of the mechanisms. We have successfully applied the same strategy based on kinetic control to cubic Pd seeds with different sizes and octahedral Pd seeds of one size to generate an array of novel bimetallic nanocrystals with well-controlled structures. With cubic Pd seeds as an example, we have also extended this strategy to the Pd-Au system. We believe this work will provide a promising route to the fabrication of bimetallic nanocrystals with novel structures and properties for applications in plasmonics, catalysis, and other areas.

Cationic monolayer-protected gold nanoparticles (AuNPs) with sizes of 6 or 2 nm interact with the cell membranes of Escherichia coli (Gram-) and Bacillus subtilis (Gram+), resulting in the formation of strikingly distinct AuNP surface aggregation patterns or lysis depending upon the size of the AuNPs. The aggregation phenomena were investigated by transmission electron microscopy and UV-vis spectroscopy. Upon proteolytic treatment of the bacteria, the distinct aggregation patterns disappeared.

Myocilin is a protein found in the extracellular matrix of the trabecular meshwork (TM) tissue, the anatomical region of the eye involved in regulating intraocular pressure. Wild-type (WT) myocilin has been associated with steroid-induced glaucoma, and variants of myocilin have been linked to early-onset, inherited glaucoma. Elevated levels and aggregation of myocilin hasten increased intraocular pressure and glaucoma-characteristic vision loss due to irreversible damage to the optic nerve. In spite of the reports of intracellular accumulation of mutant and WT myocilin in vitro, cell culture and model organisms, these aggregates have not been structurally characterized. In this work, we provide biophysical evidence for the hallmarks of amyloid fibrils in aggregated forms of WT and mutant myocilin, localized to the C-terminal olfactomedin (OLF) domain. These fibrils are grown under a variety of conditions in a nucleation dependent, self-propagating manner. Protofibrillar oligomers and mature amyloid fibrils are observed in vitro. Full-length mutant myocilin expressed in mammalian cells forms intracellular amyloid-containing aggregates as well. Taken together, this work provides new insights into and raises new questions about the molecular properties of the highly conserved OLF domain, and suggests a novel protein-based hypothesis for glaucoma pathogenesis for further testing in a clinical setting.

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