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Instruments / Technical Area	Publication Details	Published	Actions
I19-Small Molecule Single Crystal Diffraction	Encapsulation of hydrophobic pollutants within a large water-soluble [Fe4L6]4− cage Jack D. Wright , George F. S. Whitehead , Edward O. Pyzer-Knapp , Imogen A. Riddell Cell Reports Physical Science 9 DOI: 10.1016/j.xcrp.2025.102404 Diamond Proposal Number(s): [31541] Open Access Show Abstract ▼ Abstract: Hydrophobic molecules lost in water systems can have significant impacts on local ecology. Notably, the discharge of unmetabolized medications, specifically hormones, and hygiene products into effluent wastewater is a pressing environmental challenge. While selective capture of these molecules has been demonstrated by metal-organic cages (MOCs), these studies typically employ an organic solvent system that does not reflect aqueous environmental conditions. In this study, we report a rare, water-soluble, tetrahedral MOC bearing hydrosolvating sulfonate moieties alongside an aromatic naphthyl spacer. The MOC encloses a large (657 Å3) cavity that can bind a range of polycyclic structures in aqueous media. Isothermal titration calorimetry measurements support guest binding being an enthalpically driven hydrophobic binding process. The synthetic strategy employed to prepare the MOC is extensible and thus serves as a promising route to a range of large, water-soluble MOCs containing hydrophobic binding cavities with exciting prospects.	Jan 2025
	Surface-tethered planar membranes containing the β-barrel assembly machinery: A platform for investigating bacterial outer membrane protein folding Stephen C. I. Hall , Luke Clifton , Pooja Sridhar , David J. Hardy , Peter Wotherspoon , Jack Wright , James Whitehouse , Nadisha Gamage , Claire S. Laxton , Caitlin Hatton , Gareth W. Hughes , Mark Jeeves , Timothy J. Knowles Biophysical Journal DOI: 10.1016/j.bpj.2021.10.033 Show Abstract ▼ Abstract: The outer membrane of Gram-negative bacteria presents a robust physicochemical barrier protecting the cell from both the natural environment and acting as the first line of defense against antimicrobial materials. The proteins situated within the outer membrane are responsible for a range of biological functions including controlling influx and efflux. These outer membrane proteins (OMPs) are ultimately inserted and folded within the membrane by the β-barrel assembly machine (Bam) complex. The precise mechanism by which the Bam complex folds and inserts OMPs remains unclear. Here, we have developed a platform for investigating Bam-mediated OMP insertion. By derivatizing a gold surface with a copper-chelating self-assembled monolayer, we were able to assemble a planar system containing the complete Bam complex reconstituted within a phospholipid bilayer. Structural characterization of this interfacial protein-tethered bilayer by polarized neutron reflectometry (PNR) revealed distinct regions consistent with known high-resolution models of the Bam complex. Additionally, by monitoring changes of mass associated with OMP insertion by quartz crystal microbalance with dissipation monitoring (QCM-D), we were able to demonstrate the functionality of this system by inserting two diverse OMPs within the membrane, pertactin and OmpT. This platform has promising application in investigating the mechanism of Bam-mediated OMP insertion, in addition to OMP function and activity within a phospholipid bilayer environment.	Oct 2021

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