Ionic liquid (IL)-modified carbon-supported catalysts have demonstrated significant improvements in oxygen reduction reaction (ORR) activity. However, transition of this result from the half-cell to the proton exchange membrane fuel cell (PEMFC) has been challenging. Presented here is a processing methodology that yields the formation of a thin (<2 nm) conformal IL coating on the surface of both three-dimensional electrocatalysts and bulk single crystals through the sequential capacitive deposition (SCD) of anionic and cationic components and their subsequent condensation into a hydrophobic, protic IL. SCD shows promise for IL incorporation into preformed PEMFC catalyst layers.

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Malaria, the world's most devastating parasitic disease, is transmitted between humans by mosquitoes of the Anopheles genus. An. gambiae is the principal malaria vector in Sub-Saharan Africa. The C-type lectins CTL4 and CTLMA2 cooperatively influence Plasmodium infection in the malaria vector Anopheles. Here we report the purification and biochemical characterization of CTL4 and CTLMA2 from An. gambiae and An. albimanus. CTL4 and CTLMA2 are known to form a disulfide-bridged heterodimer via an N-terminal tri-cysteine CXCXC motif. We demonstrate in vitro that CTL4 and CTLMA2 intermolecular disulfide formation is promiscuous within this motif. Furthermore, CTL4 and CTLMA2 form higher oligomeric states at physiological pH. Both lectins bind specific sugars, including glycosaminoglycan motifs with β1-3/β1-4 linkages between glucose, galactose and their respective hexosamines. Smallangle x-ray scattering data supports a compact heterodimer between the CTL domains. Recombinant CTL4/CTLMA2 is found to function in vivo, reversing the enhancement of phenol oxidase activity in dsCTL4-treated mosquitoes. We propose these molecular features underline a common function for CTL4/CTLMA2 in mosquitoes, with species and strain-specific variation in degrees of activity in response to Plasmodium infection. The innate immune response of An. gambiae to malaria parasites (genus Plasmodium) in an infectious blood meal is a significant factor influencing the prevalence and vectoral capacity of mosquitoes in a population 1,2. Understanding the molecular interactions and mechanisms of Anopheles immunity is therefore key to comprehending, predicting, and potentially controlling disease transmission. An. gambiae has a complement-like immune response centered upon thioester-containing protein 1 (TEP1) that effectively targets Plasmodium ookinetes following their traversal of the midgut epithelium, prior to their transformation into oocysts 3-7. The immune response to Plasmodium involves additional proteins such as the leucine-rich immune molecule (LRIM) family 8 , CLIP proteases 9 , and other families. Two LRIM family members, LRIM1 and APL1C, form a heterodimeric complex that directly interacts with TEP1 to regulate its anti-Plasmodium activity 10-12. Yet the extent of interactions between these and other immune factors and mechanistic details of the mosquito immune response remain in large part unknown. The C-type lectin (CTL) fold is the most common binding site for glycans, their special feature being a lectin-bound Ca 2+ ion in direct coordination with the bound sugar 13-15. The CTL domain (CTLD), or C-type carbohydrate recognition domain (CRD), consists of ~130 amino acids with a five-stranded antiparallel β-sheet and two α-helices. Four cysteines within the CTLD form two disulfide bonds that stabilize the fold. The Ca 2+ binding

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Exposure to TiO2 results in a ∼8-fold increase in bacterial Ti content, with concomitant changes in quotas of other biometals.