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Instruments / Technical Area	Publication Details	Published
B23-Circular Dichroism	Multi-enzyme cascade reactions using protein–polymer surfactant self-standing films Thomas Farrugia , Adam W. Perriman , Kamendra Sharma , Stephen Mann Chemical Communications DOI: 10.1039/C6CC09809F Diamond Proposal Number(s): [11932] Show Abstract ▼ Abstract: Hierarchical self-assembly is used to fabricate bio-catalytically active, self-supporting protein–polymer surfactant films capable of sustaining two- or three-enzyme cascade reactions.	Jan 2017
B23-Circular Dichroism I22-Small angle scattering & Diffraction	Enzyme activity in liquid lipase melts as a step towards solvent-free biology at 150°C Alex P. S. Brogan , Kamendra P. Sharma , Adam W. Perriman , Stephen Mann Nature Communications 5 DOI: 10.1038/ncomms6058 Diamond Proposal Number(s): [9731] Show Abstract ▼ Abstract: Water molecules play a number of critical roles in enzyme catalysis, including mass transfer of substrates and products, nucleophilicity and proton transfer at the active site, and solvent shell-mediated dynamics for accessing catalytically competent conformations. The pervasiveness of water in enzymolysis therefore raises the question concerning whether biocatalysis can be undertaken in the absence of a protein hydration shell. Lipase-mediated catalysis has been undertaken with reagent-based solvents and lyophilized powders, but there are no examples of molecularly dispersed enzymes that catalyse reactions at sub-solvation levels within solvent-free melts. Here we describe the synthesis, properties and enzyme activity of self-contained reactive biofluids based on solvent-free melts of lipase-polymer surfactant nanoconjugates. Desiccated substrates in liquid (p-nitrophenyl butyrate) or solid (p-nitrophenyl palmitate) form can be mixed or solubilized, respectively, into the enzyme biofluids, and hydrolysed in the solvent-free state. Significantly, the efficiency of product formation increases as the temperature is raised to 150 °C.	Oct 2014
B23-Circular Dichroism	Self-organization of glucose oxidase-polymer surfactant nanoconstructs in solvent-free soft solids and liquids Kamendra Sharma , Yixiong Zhang , Michael R. Thomas , Alex Brogan , Adam Perriman , Stephen Mann The Journal Of Physical Chemistry B 118 (39), 11573 - 11580 DOI: 10.1021/jp507566u Diamond Proposal Number(s): [8467] Show Abstract ▼ Abstract: An anisotropic glucose oxidase–polymer surfactant nanoconjugate is synthesized and shown to exhibit complex temperature-dependent phase behavior in the solvent-free state. At close to room temperature, the nanoconjugate crystallizes as a mesolamellar soft solid with an expanded interlayer spacing of ca. 12 nm and interchain correlation lengths consistent with alkyl tail–tail and PEO–PEO ordering. The soft solid displays a birefringent spherulitic texture and melts at 40 °C to produce a solvent-free liquid protein without loss of enzyme secondary structure. The nanoconjugate melt exhibits a birefringent dendritic texture below the conformation transition temperature (Tc) of glucose oxidase (58 °C) and retains interchain PEO–PEO ordering. Our results indicate that the shape anisotropy of the protein–polymer surfactant globular building block plays a key role in directing mesolamellar formation in the solvent-free solid and suggests that the microstructure observed in the solvent-free liquid protein below Tc is associated with restrictions in the intramolecular motions of the protein core of the nanoconjugate.	Oct 2014
B21-High Throughput SAXS B23-Circular Dichroism	Redox transitions in an electrolyte-free myoglobin fluid Kamendra Sharma , Kieren Bradley , Alex P. S. Brogan , Stephen Mann , Adam W. Perriman , David J. Fermin Journal Of The American Chemical Society 135 (49), 18311 - 18314 DOI: 10.1021/ja4104606 Diamond Proposal Number(s): [8467, 9361, 7504, 7828] Show Abstract ▼ Abstract: Redox responses associated with the heme prosthetic group in a myoglobin-polymer surfactant solvent-free liquid are investigated for the first time in the absence of an electrolyte solution. Cyclic voltammograms from the biofluid exhibit responses that are consistent with planar diffusion of mobile charges in the melt. Temperature-dependent dynamic electrochemical and rheological responses are rationalized in terms of the effective electron hopping rate between heme centers and the transport of intrinsic ionic species in the viscous protein liquid.	Dec 2013

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