A Grubbs-Hoveyda type catalyst with a N-pentiptycenyl, N-cyclohexyl-NHC ligand provides poly(nbe-alt-coe) with an excellent degree of alternation while lacking significant activity in the homopolymerization of cyclooctene.

This contribution focuses on understanding of paper wet-strength properties, by taking a closer look at the spatial distribution of wet-strengthening polymers inside the cellulosic fiber network deposited under different treatment conditions using confocal laser scanning microscopy as in situ imaging tool. We compare the behavior of paper samples treated with a photochemically cross-linkable copolymer using an impregnation process employing three different solvents, namely water, 2-propanol (IPA) and 1-butanol (BuOH), respectively. As these solvents swell paper fibers to quite different extents, the deposition of the polymer, on, in or in-between the cellulosic fibers varies quite strongly, as is shown by in-depth analysis using confocal laser scanning microscopy. The difference in accessibility of distinct surface sites exclusively on or also in and between the fibers controls the macroscopic tensile strength under both dry and wet conditions.

Microfluidic paper combines pump-free water transport at low cost with a high degree of sustainability, as well as good availability of the paper-forming cellulosic material, thus making it an attractive candidate for point-of-care (POC) analytics and diagnostics. Although a number of interesting demonstrators for such paper devices have been reported to date, a number of challenges still exist, which limit a successful transfer into marketable applications. A strong limitation in this respect is the (unspecific) adsorption of protein analytes to the paper fibers during the lateral flow assay. This interaction may significantly reduce the amount of analyte that reaches the detection zone of the microfluidic paper-based analytical device (µPAD), thereby reducing its overall sensitivity. Here, we introduce a novel approach on reducing the nonspecific adsorption of proteins to lab-made paper sheets for the use in µPADs. To this, cotton linter fibers in lab-formed additive-free paper sheets are modified with a surrounding thin hydrogel layer generated from photo-crosslinked, benzophenone functionalized copolymers based on poly-(oligo-ethylene glycol methacrylate) (POEGMA) and poly-dimethyl acrylamide (PDMAA). This, as we show in tests similar to lateral flow assays, significantly reduces unspecific binding of model proteins. Furthermore, by evaporating the transport fluid during the microfluidic run at the end of the paper strip through local heating, model proteins can almost quantitatively be accumulated in that zone. The possibility of complete, almost quantitative protein transport in a µPAD opens up new opportunities to significantly improve the signal-to-noise (S/N) ratio of paper-based lateral flow assays.