6 results for Brimble, Margaret, Conference poster

  • The Effect of Glycosylation on the Potency of Pramlintide, An Anti-Diabetic Drug

    Fletcher, Madeleine; Kowalczyk, Renata; Fairbanks, A; Brimble, Margaret; Hay, DL (2013-12-18)

    Conference poster
    The University of Auckland Library

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  • A synthetic study towards aryl 6,6-spiroacetal analogues of rubromycin

    Choi, Peter; Rathwell, DC; Brimble, Margaret (2008)

    Conference poster
    The University of Auckland Library

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  • Investigation into the racemic X-ray structure of the antimicrobial protein snakin-1

    Yeung, Ho; Yosaatmadja, Yuliana; Squire, Christopher; Harris, Paul; Baker, Edward; Brimble, Margaret (2015-10-22)

    Conference poster
    The University of Auckland Library

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  • Investigation into the racemic X-ray structure of the antimicrobial protein snakin-1

    Yeung, Ho; Yosaatmadja, Yuliana; Squire, Christopher; Harris, Paul; Baker, Edward; Brimble, Margaret (2015-08-31)

    Conference poster
    The University of Auckland Library

    Snakin-1 is a 63 residue antimicrobial protein originally isolated from potato (Solanum tuberosum).1 It is active against a number of bacterial and fungal phytopathogens such as Clavibacter michiganensis, Pseudomonas syringae and Fusarium solani. Snakin-1 is a member of the GASA (gibberellic acid stimulated in Arabidopsis)/snakin family and the mature protein consists of a GASA domain incorporating six intramolecular disulfide bonds.2 The amino acid sequences of these proteins do not correspond to any known structural motifs. GASA/snakin proteins are found in a variety of plant species and appear to be involved in a range of functions including cell elongation and cell division.2 Their expression profiles support these roles and are commonly linked to development.2 It has also been speculated that the 12 conserved cysteines in these proteins perform a role in redox regulation.2 We have recently completed the total chemical synthesis of native Snakin-1 and showed that its antimicrobial activity is comparable to that of the naturally occurring protein.3 In an attempt to understand how this small protein functions we have determined its threedimensional structure by X-ray crystallography using a quasi-racemic protein system.4 Phase information for structural determination was obtained by radiation-damage induced phasing.5 The structure of snakin-1 appears to be novel, different to known classes of cysteine-rich plant antimicrobial peptide. Its features include a large and distinctly electropositive loop that we speculate to be membrane targeting, and a two helix bundle which is a potential membrane-interacting feature able to disrupt the structural integrity of its target bacteria.

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  • Targeting synthetic glycopeptides to MGL on Dermal Dendritic cells

    McIntosh, Julie; Angel, CE; Chen, CJJ; Manning, K; Mansell, Claudia; Agrawai, S; Harris, Paul; Williams, Geoffrey; Squire, Christopher; Brimble, Margaret; Dunbar, Peter (2011-02-14)

    Conference poster
    The University of Auckland Library

    The ability of a peptide vaccine to stimulate T cells in vivo might be improved by specifically targeting the peptide to dendritic cells (DC). The C-type lectin Macrophage Galactose-type lectin, MGL (CD301), has been shown to bind to N-acetyl-galactosamine (GalNAc) and small peptides bearing O-linked GalNAc. Synthetic GalNAc can be produced using relatively simple organic chemistry when compared with the complicated branched sugars that are recognised by other C-type lectins. MGL therefore represents a promising target for the design of synthetic peptide vaccines. We have identified that antigen-presenting cells in human skin express MGL and have confirmed that CD14+ dermal DCs might be targeted via MGL. The intracellular fate of MGL following internalisation was tracked by confocal microscopy. MGL traffics through early endosomes to late endosomes/lysosomes, and colocalises with MHC class I and class II. Synthetic glycopeptides were produced incorporating either native O-linked GalNAc or GalNAc residues linked to the peptide chain via non-native ???Click??? chemistry. Biophysical analysis of the ability of both ???Click??? and native glycopeptides peptides with recombinant MGL confirmed the ability of both these peptides to bind MGL. Ongoing work aims to determine whether targeting to MGL using these synthetic peptides results in efficient presentation of antigen to T cells.

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  • Effects of a self-adjuvanting Synthetic Long Peptide targeting TLR2 on human immune cells

    Burkert, Kristina; Mansell, Claudia; McIntosh, Julie; Brooks, Anna; Angel, Catherine; Winkler, S; Harris, Paul; Williams, Geoffrey; Brimble, Margaret; Dunbar, Peter (2010-10-27)

    Conference poster
    The University of Auckland Library

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