Electrically conductive adhesives (ECA’s) are used widely to replace or reinforce lead soldering or conductive metal components in electronic packaging applications such as die attachment, solderless interconnections, component repair, display interconnections, and heat dissipation. Their conductive behavior as well as the associated behaviors such as heat conduction and mechanical behavior (strength, rigidity, deformation and viscoelastic behavior, which may be affected by moisture ingression) are affected by adhesive film thickness, volume fraction, size and shape of the conductive filler, as well as uncured base adhesive viscosity, substrate and filler surface treatment and the applied pressure (during bonding and during conduction). The adhesive resistivity decreases precipitously above a characteristic filler volume fraction called the percolation threshold. In general, micron-sized metal fillers mixed in an adhesive (often an epoxy) resulting with different film thicknesses exhibit thickness thresholds for transition from three-dimensional conductivity to two-dimensional conductivity with considerable increases in thickness-direction (z-axis) resistivity when the film thicknesses are smaller than these threshold values. Recently, the use of conductive nanoparticles allowed decreases in percolation threshold levels as well as increases in mechanical strength and durability of ECA’s. Most ECA’s are supplied in liquid or paste form in varying viscosities and therefore, the method of their application also affects their performance. This work intends to provide an understanding of these effects on conduction behavior in (usually high-priced) equipment in which they are used.

Breast cancer is the most common cancer in women globally, often necessitating mastectomy and subsequent breast reconstruction. Silicone mammary implants (SMIs) play a pivotal role in breast reconstruction, yet their interaction with the host immune system and microbiome remains poorly understood. This study investigates the impact of SMI surface topography on host antimicrobial responses, wound proteome dynamics, and microbial colonization. Biological samples were col-lected from ten human patients undergoing breast reconstruction with SMIs. Mass spectrometry profiles were analyzed for acute and chronic wound proteomes, revealing a nuanced interplay between topography and antimicrobial respondseproteins. 16S rRNA sequencing assessed mi-crobiome dynamics, unveiling topography-specific variations in microbial composition. Surface topography alterations influenced wound proteome composition. Microbiome analysis revealed heightened diversity around rougher SMIs, emphasizing topography-dependent microbial inva-sion. In vitro experiments confirmed staphylococcal adhesion, growth, and biofilm formation on SMI surfaces, with increased texture correlating positively with bacterial colonization. This comprehensive investigation highlights the intricate interplay between SMI topography, wound proteome dynamics, and microbial transmission. The findings contribute to understanding host-microbe interactions on SMI surfaces, essential for optimizing clinical applications and minimizing complications in breast reconstruction.

The affinity constant, also known as the equilibrium constant, binding constant, equilibrium association constant, or the reciprocal value, the equilibrium dissociation constant (K_d), can be considered as one of the most important characteristics for any antibody-antigen pair. Many methods based on different technologies have been proposed and used to determine this value. However, since a very large number of publications and commercial datasheets do not include this information, significant obstacles in performing such measurements seem to exist. In other cases where such data are reported, the results have often proved to be unreliable. This situation may indicate that most of the technologies available today require a high level of expertise that does not seem to be available in many laboratories. In this paper, we present a simple approach based on standard immunoassay technology that is easy and quick to perform. It relies on the effect that the molar IC₅₀ approaches the K_d value in the case of infinitely small concentrations of the reagent concentrations. A two-dimensional dilution of the reagents leads to an asymptotic convergence to K_d. The approach has some similarity to the well-known checkerboard titration used for the optimization of immunoassays. A well-known antibody against the FLAG peptide, clone M2, was used as a model system and the results were compared with other methods. This approach could be used in any case where a competitive assay is available or can be developed. The determination of an affinity constant should belong to the crucial parameters in any quality control of antibody-related products and assays and should be mandatory in papers using immunochemical protocols.