tological findings and activation of the acute inflammatory response when using the higher MB dose. The potential activation of the inflammatory response following ultrasound-mediated BBB opening should be considered when treating patients to maximize therapeutic benefit.In an effort to combine the anti-proliferative effect of CUR-BF2 and CUR compounds with anti-inflammatory benefits of non-steroidal anti-inflammatory drugs (NSAIDs), a library of the bis- and mono-NSAID/CUR-BF2 and NSAID/CUR conjugates were synthesized by coupling flufenamic acid, flurbiprofen, naproxen, indomethacin, and ibuprofen to diversely substituted hydroxy-benzaldehydes via an ester linkage, and by subsequent reaction with acetylacetone-BF2 to form the bis- and the mono-NSAID/CUR-BF2 adducts. Since conversion to NSAID/CUR by the previously developed decomplexation protocol showed limited success, a set of NSAID/CUR conjugates were independently prepared by directly coupling the NSAIDs with parent curcumin. The bis-NSAID/CUR-BF2 and bis-NSAID-CUR hybrids exhibited low cytotoxicity in NCI-60 assay, and in independent cell viability assay on colorectal cancer (CRC) cells (HCT116, HT29, DLD-1, RKO, SW837, CaCo2) and in normal CR cells (CCD841CoN). By contrast, the mono-naproxin and mono-flurbiprofen CUR-BF2 adducts exhibited remarkable anti-proliferative and apoptopic activity in NCI-60 assay most notably against HCT-116 (colon), OVCAR-3 (ovarian), and ACHN (renal) cells. Computational molecular docking calculations showed favorable binding energies to HER2, VEGFR2, BRAF, and Bcl-2 as well as to COX-1 and COX-2, which in several cases exceeded known inhibitors. The main interactions between the ligands and the proteins were hydrophobic, although several hydrogen bonds were also observed. A sub-set of six compounds that had exhibited little or no cytotoxicity were tested for their anti-inflammatory response with THP-1 human macrophages in comparison to parent NSAIDs or parent curcumin.The Experimental Lakes Area in Northwestern Ontario, Canada, is a globally prominent freshwater research facility, conducting impactful whole-of-lake experiments on so-called ‘pristine’ lakes and watersheds. These lakes are located in traditional Anishinaabe (Indigenous) territory and the home of 28 Treaty #3 Nations, something rarely acknowledged until now. Indeed, Indigenous peoples in the area have historically been excluded from the research facility’s governance and research. Shortly after it changed hands in 2014-from the federal government to the not-for-profit International Institute of Sustainable Development (IISD)-the Truth and Reconciliation Commission (TRC) of Canada released its Calls to Action to all Canadians. selleck products The newly named International Institute of Sustainable Development-Experimental Lakes Area (IISD-ELA) began to respond with a number of initiatives aimed to develop relationships with local Indigenous peoples and communities. In this paper, from the perspectives of IISD-ELA staff members, we share findings from an exploratory study into the relationships beginning to develop between IISD-ELA and Treaty #3 Nations. We used semi-structured interviews (n = 10) to identify how staff perceived their initial efforts and contextualize those with the current literature on meaningfully engagement in reconciliation. Our analysis highlights perceived barriers, including time, resources, and funding constraints, as well as an acknowledged lack of cultural awareness and sensitivity training. Participants also recognized the need to engage Indigenous knowledge holders and embrace their ways of knowing at the research station. While the study is small in scale, as an international leader in freshwater science, transparency in the IISD-ELA’s journey in reconciliation has the potential to inform, influence, and ‘unsettle’ settler-colonial scientists, field stations, and institutions across the country and beyond.Effluents of textile, paper, and related industries contain significant amounts of synthetic dyes which has serious environmental and health implications. Remediation of dyes through physical and chemical techniques has specific limitations. Augmented biological decontamination strategies ‘microbial remediation’ may involve ring-opening of dye molecules besides the reduction of constituent metal ions. Both bacterial and fungal genera are known to exhibit metabolic versatility which can be harnessed for effective bio-removal of the toxic dye contaminants. Ascomycetous/basidiomycetes fungi can effectively decontaminate azo dyes through laccase/peroxidase enzyme-mediated catalysis. The extent, efficacy, and range of fungal dye decontamination can be enhanced by the conjugated application of nanomaterials, including nanoparticles (NPs) and their composites. Fungal cell-enabled NP synthesis- ‘myco-farmed NPs’, is a low-cost strategy for scaled-up fabrication of a variety of metal, metal oxide, non-metal oxide NPs through oxidation/reduction of dissolved ions/molecules by extracellular biomolecules. Augmented and rapid decontamination of azo dyes at high concentrations can be achieved by the use of myco-farmed NPs, NPs adsorbed fungal biomass, and nano-immobilized fungi-derived bio-catalytical agents. This manuscript will explore the opportunities and benefits of mycoremediation and application of fungus-NP bionanoconjugate to remediate dye pollutants in wastewaters and land contaminated with the effluent of textile industries.4-Coumarate coenzyme A ligase (4CL) is a key enzyme involved in the early steps of the monolignol biosynthetic pathway. It is hypothesized to modulate S and G monolignol content in the plant. Lignin removal is imperative to the paper industry and higher S/G ratio governs better extractability of lignin and economics of the pulping process. This background prompted us to predict 3D structure of two isoforms of 4CL in Leucaena leucocephala and evaluate their substrate preferences. The 3D structure of Ll4CL1 and Ll4CL2 protein were created by homology modeling and further refined by loop refinement. Molecular docking studies suggested differential substrate preferences of both the isoforms. Ll4CL1 preferred sinapic acid (- 4.91 kcal/mole), ferulic acid (- 4.84 kcal/mole), hydroxyferulic acid (- 4.72 kcal/mole), and caffeic acid (- 4.71 kcal/mole), in their decreasing order. Similarly, Ll4CL2 preferred caffeic acid (- 6.56 kcal/mole, 4 H bonds), hydroxyferulic acid (- 6.56 kcal/mole, 3 H bonds), and ferulic acid (- 6.