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Mansell, T. J.

Publications and source records attributed to Mansell, T. J..

2 recordsLinked to original sources

Structural and Metabolic Characterization of Ni(I)-inhibitors Provide a Robust Anti-Methanogenicity Scoring System

Atmospheric methane (CH4) acts as a key contributor to global warming and a short-lived climate forcer. CH4 mitigation represents the most promising means to address short-term climate change. Ruminant enteric CH4 produced by methanogenic archaea represents 27.2% of global CH4 emissions. Only a few of the direct methanogenesis inhibitors identified bear high mitigation potential hence it is important to investigate their underlying modes of action. Here, we elucidated biophysical and thermodynamic interplay between known inhibitors and cofactor F430, to determine their stoichiometric ratios and binding affinities. We leverage this prior in a robust contrastive learning approach to functionally cluster known sixteen inhibitors and 53,959 bovine-linked metabolites. We demonstrate a multi-factor optimization protocol to identify putative inhibitors with: (i) high bacterial membrane permeability, (ii) no adverse effect to ruminal fermentation, (iii) known degradation pathway, and (iv) direct commercial availability. Subsequent in vitro assays and community metabolic modeling with a first set of eight treatment molecules revealed structo-metabolic priors that tie thermodynamic signatures of inhibition to metabolic flux shifts. We established a multi-scale workflow that transforms ostensibly negative compounds into mechanistic insight, linking rumen metabolic flux shifts to MCR-F430-Ni(I) inhibition chemistry as a foundation for rational methane-mitigation design. COVER ABSTRACT O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=147 SRC="FIGDIR/small/708075v1_ufig1.gif" ALT="Figure 1"> View larger version (40K): org.highwire.dtl.DTLVardef@1d38d21org.highwire.dtl.DTLVardef@1d681d9org.highwire.dtl.DTLVardef@1e70c0corg.highwire.dtl.DTLVardef@1c8223f_HPS_FORMAT_FIGEXP M_FIG C_FIG

systems biology↗

Paper-based Sensing of Fucosylated Biological Compounds

Advances in sensing technology have enabled rapid analysis of various biomolecules including complex carbohydrates. However, glycan analysis is limited by the throughput and complexity of assays for quantifying them. We describe a simple, low-cost enzymatic assay for the rapid analysis of fucosylation, down to linkage specificity, and its application to high-throughput screening of biologically relevant fucosylated compounds, to facilitate simple and straightforward analytical techniques. Paper-based devices integrate biosensor platforms and other diagnostic assays by fusing them with wax printing technology, making their fabrication even more inexpensive and simple. The specificity of the assay is established by linkage-specific glycosidic enzymes and the colorimetric output is visible to the naked eye, with costs that are lower than fluorescence/luminescence-based assays ($0.02/reaction). This platform was further improved by enhancing storage stability to retain analytical performance over time using desiccation and freeze-drying techniques. The assay platform allows analysis of hundreds of samples in minutes and we anticipate that this rapid and simple analytical method will be extended towards developing a universal glyco-barcoding platform for high throughput screening of glycosylation.

biochemistry↗