Biomimetic layer-by-layer assembly of artificial nacre.

Nacre is a technologically remarkable organic-inorganic composite biomaterial. It consists of an ordered multilayer structure of crystalline calcium carbonate platelets separated by porous organic layers. This microstructure exhibits both optical iridescence and mechanical toughness, which transcend those of its constituent components. Replication of nacre is essential for understanding this complex biomineral, and paves the way for tough coatings fabricated from cheap abundant materials. Fabricating a calcitic nacre imitation with biologically similar optical and mechanical properties will likely require following all steps taken in biogenic nacre synthesis. Here we present a route to artificial nacre that mimics the natural layer-by-layer approach to fabricate a hierarchical crystalline multilayer material. Its structure-function relationship was confirmed by nacre-like mechanical properties and striking optical iridescence. Our biomimetic route uses the interplay of polymer-mediated mineral growth, combined with layer-by-layer deposition of porous organic films. This is the first successful attempt to replicate nacre, using CaCO(3).

Relationship between prion propensity and the rates of individual molecular steps of fibril assembly.

Peptides and proteins possess an inherent propensity to self-assemble into generic fibrillar nanostructures known as amyloid fibrils, some of which are involved in medical conditions such as Alzheimer disease. In certain cases, such structures can self-propagate in living systems as prions and transmit characteristic traits to the host organism. The mechanisms that allow certain amyloid species but not others to function as prions are not fully understood. Much progress in understanding the prion phenomenon has been achieved through the study of prions in yeast as this system has proved to be experimentally highly tractable; but quantitative understanding of the biophysics and kinetics of the assembly process has remained challenging. Here, we explore the assembly of two closely related homologues of the Ure2p protein from Saccharomyces cerevisiae and Saccharomyces paradoxus, and by using a combination of kinetic theory with solution and biosensor assays, we are able to compare the rates of the individual microscopic steps of prion fibril assembly. We find that for these proteins the fragmentation rate is encoded in the structure of the seed fibrils, whereas the elongation rate is principally determined by the nature of the soluble precursor protein. Our results further reveal that fibrils that elongate faster but fracture less frequently can lose their ability to propagate as prions. These findings illuminate the connections between the in vitro aggregation of proteins and the in vivo proliferation of prions, and provide a framework for the quantitative understanding of the parameters governing the behavior of amyloid fibrils in normal and aberrant biological pathways.