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The ability of a phosphine-appended-2,2′-bipyridine ligand ((Ph 2 P) 2 bpy) to serve as a platform for late-stage ligand modifications was evaluated using tetrahedral (Ph 2 P) 2 bpyFeCl 2 . We employed a post-metalation Staudinger reaction to install a series of functionalized arenes, including those containing Brønsted and Lewis acidic groups. This reaction sequence represents a versatile strategy to both tune the ligand donor properties as well as directly incorporate appended functionality. 

Diffusiophoresis is the spontaneous movement of colloidal particles in a concentration gradient of solutes. As a small-scale phenomenon that harnesses energy from concentration gradients, diffusiophoresis may prove useful for passively manipulating particles in lab-on-a-chip applications as well as configurations involving interfaces. Though naturally occurring ions are often multivalent, experimental studies of diffusiophoresis have been mostly limited to monovalent electrolytes. In this work, we investigate the motion of negatively charged polystyrene particles in one-dimensional salt gradients for a variety of multivalent electrolytes. We develop a one-dimensional model and obtain good agreement between our experimental and modeling results with no fitting parameters. Our results indicate that the ambipolar diffusivity, which is dependent on the valence combination of cations and anions, dictates the speed of the diffusiophoretic motion of the particles by controlling the time scale at which the electrolyte concentration evolves. In addition, the ion valences also modify the electrophoretic and chemiphoretic contributions to the diffusiophoretic mobility of the particles. Our results are applicable to systems where the chemical concentration gradient is comprised of multivalent ions, and motivate future research to manipulate particles by exploiting ion valence. 

Recombinant protein production plays an essential role in both biological studies and pharmaceutical production. Escherichia coli is one of the most favorable hosts for this purpose. Although a number of strategies for optimizing protein production have been developed, the effect of gene overexpression on host cell growth has been much less studied. Here, we performed high-throughput tests on the E. coli a complete set of E. coli K-12 ORF archive (ASKA) collection to quantify the effects of overexpressing individual E. coli genes on its growth. The results indicated that overexpressing membrane-associated proteins or proteins with high abundances of branched-chain amino acids tended to impair cell growth, the latter of which could be remedied by amino acid supplementation. Through this study, we expect to provide an index for a fast pre-study estimate of host cell growth in order to choose proper rescuing approaches when working with different proteins.