High-throughput micro-nanostructuring by microdroplet inkjet printing

The production of micrometer-sized structures comprised of nanoparticles in defined patterns and densities is highly important in many fields, ranging from nano-optics to biosensor technologies and biomaterials. A well-established method to fabricate quasi-hexagonal patterns of metal nanoparticles is block copolymer micelle nanolithography, which relies on the self-assembly of metal-loaded micelles on surfaces by a dip-coating or spin-coating process. Using this method, the spacing of the nanoparticles is controlled by the size of the micelles and by the coating conditions. Whereas block copolymer micelle nanolithography is a high-throughput method for generating well-ordered nanoparticle patterns at the nanoscale, so far it has been inefficient in generating a hierarchical overlay structure at the micrometer scale. Here, we show that by combining block copolymer micelle nanolithography with inkjet printing, hierarchical patterns of gold nanoparticles in the form of microstructures can be achieved in a high-throughput process. Inkjet printing was used to generate droplets of the micelle solution on surfaces, resulting in printed circles that contain patterns of gold nanoparticles with an interparticle spacing between 25 and 42 nm. We tested this method on different silicon and nickel–titanium surfaces and the generated patterns were found to depend on the material type and surface topography. Based on the presented strategy, we were able to achieve patterning times of a few seconds and produce quasi-hexagonal micro-nanopatterns of gold nanoparticles on smooth surfaces. Hence, this method is a high-throughput method that can be used to coat surfaces with nanoparticles in a user-defined pattern at the micrometer scale. As the nanoparticles provide a chemical contrast on the surface, they can be further functionalized and are therefore highly relevant for biological applications

The threshold of amyloid aggregation of beta-lactoglobulin : Relevant factor combinations

This study identifies critical factor combinations of pH, temperature, stirring speed, protein and ion concentration that specifically affect the lag-, and growth phase of beta-lactoglobulin amyloid aggregation and provides information on how, when and why certain factor combinations affect the onset of amyloid aggregation. Conditions at the threshold of amyloid formation were chosen to prolong the lag and growth phase for several hours. Temperature was the most important factor in all aggregation stages. Interactions between low pH and temperature in the growth phase were caused by elevated protein denaturation at low pH (DSC). Interactions between stirring speed and temperature in the lag phase were caused by viscosity-dependent shear stress (CFD-simulation). Even if none of the factor combinations could shift the onset of amyloid aggregation, important factor combinations were identified that favour the onset of amyloid aggregation. Therefore, the results of this study could be relevant for industrial production.</p

Influence of the polydispersity of pH 2 and pH 3.5 beta-lactoglobulin amyloid fibril solutions on analytical methods

It is well known that amyloid beta-lactoglobulin (BLG) fibril solutions contain a heterogeneous mixture of amyloid aggregates and non-amyloid material. However, few information are available on how strongly separated fractions of different morphologies (straight fibrils at pH 2 and worm-like aggregates at pH 3.5) vary with respect to physicochemical properties and building blocks as most analyses are conducted with unfractionized solutions where superposition effects occur. The pH-value shift resulted in an altered degree of acid hydrolysis which led to dissimilar building blocks of the aggregates (peptides at pH 2, non-hydrolyzed protein at pH 3.5). The respective separated amyloid and non-amyloid fractions showed significantly different size (SAXS, SEC, AUC) and charge properties (Zeta potential) than the whole samples. Strong superposition effects were evident with common analyses such as FTIR, TRP fluorescence and Thioflavin-T. At the same time, structural differences of pH 2 and pH 3.5 aggregates could be presented more clearly.</p