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Instruments / Technical Area	Publication Details	Published
I07-Surface & interface diffraction	The role of protein hydrophobicity in thioninphospholipid interactions: a comparison of alpha 1 and alpha 2-purothionin adsorbed anionic phospholipid monolayers Luke Clifton , Michael Sanders , Christy Kinane , Tom Arnold , Karen J. Edler , Cameron Neylon , Rebecca Green , Richard Frazier Physical Chemistry Chemical Physics 14 (39), 13569-13579 DOI: 10.1039/c2cp42029e Diamond Proposal Number(s): [6306] Show Abstract ▼ Abstract: The plant defence proteins ?1- and ?2-purothionin (Pth) are type 1 thionins from common wheat (Triticum aestivum). These highly homologous proteins possess characteristics common amongst antimicrobial peptides and proteins, that is, cationic charge, amphiphilicity and hydrophobicity. Both ?1- and ?2-Pth possess the same net charge, but differ in relative hydrophobicity as determined by C18 reversed phase HPLC. Brewster angle microscopy, X-ray and neutron reflectometry, external reflection FTIR and associated surface pressure measurements demonstrated that ?1 and ?2-Pth interact strongly with condensed phase 1,2-dipalmitoyl-sn-glycero-3-phospho-(1?-rac-glycerol) (DPPG) monolayers at the air/liquid interface. Both thionins disrupted the in-plane structure of the anionic phospholipid monolayers, removing lipid during this process and both penetrated the lipid monolayer in addition to adsorbing as a single protein layer to the lipid head-group. However, analysis of the interfacial structures revealed that the ?2-Pth showed faster disruption of the lipid film and removed more phospholipid (12%) from the interface than ?1-Pth. Correlating the protein properties and lipid binding activity suggests that hydrophobicity plays a key role in the membrane lipid removal activity of thionins.	Aug 2012
B23-Circular Dichroism	Introducing Structural Flexibility Into Porphyrin-DNA Zipper Arrays Eugen Stulz , Ashley Brewer , Guiliano Siligardi , Cameron Neylon Organic & Biomolecular Chemistry 9, 777-782 DOI: 10.1039/c0ob00535e Diamond Proposal Number(s): [1815] Show Abstract ▼ Abstract: A more flexible nucleotide building block for the synthesis of new DNA based porphyrinzipper arrays is described. Changing the rigid acetylene linker between the porphyrin substituent and the 2′-deoxyuridine to a more flexible propargyl amide containing linkage leads in part to an increased duplex stability. The CD spectra reveal different electronic interactions between the porphyrins depending on the type of linker used. Molecular modelling suggests large variation of the relative orientation of the porphyrins within the major groove of the DNA. The porphyrins can be metallated post-synthetically with different metals as shown with zinc, cobalt and copper. The spectroscopic features do not alter drastically upon metallation apart from the CD spectra, and the stability of the metal complex is highly dependent on the nature of the metal. As shown by CD spectroscopy, the zinc porphyrin is rapidly demetallated at high temperatures. Globular structure determination using SAXS indicates that a molecular assembly comprised of a two to four helical bundle dominates in solution at higher concentrations (≥50 μM) which is not observed by spectroscopy at lower concentrations (≤1 μM).	Mar 2011
B23-Circular Dichroism	Energy Transfer & Self-Assembly of DNA based Nano-Structures Jon Burns , Guiliano Siligardi , Cameron Neylon , Eugen Stulz	Nov 2010

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