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Selected wheat seed defense proteins exhibit competitive binding to model microbial lipid interfaces

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Sanders, M. R., Clifton, L. A., Neylon, C., Frazier, R. A. and Green, R. J. (2013) Selected wheat seed defense proteins exhibit competitive binding to model microbial lipid interfaces. Journal of Agricultural and Food Chemistry, 61 (28). pp. 6890-6900. ISSN 1520-5118

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To link to this item DOI: 10.1021/jf401336a

Abstract/Summary

Puroindolines (Pins) and purothionins (Pths) are basic, amphiphilic, cysteine-rich wheat proteins that play a role in plant defense against microbial pathogens. We have examined the co-adsorption and sequential addition of Pins (Pin-a, Pin-b and a mutant form of Pin-b with Trp-44 to Arg-44 substitution) and β-purothionin (β-Pth) model anionic lipid layers, using a combination of surface pressure measurements, external reflection FTIR spectroscopy and neutron reflectometry. Results highlighted differences in the protein binding mechanisms, and in the competitive binding and penetration of lipid layers between respective Pins and β-Pth. Pin-a formed a blanket-like layer of protein below the lipid surface that resulted in the reduction or inhibition of β-Pth penetration of the lipid layer. Wild-type Pin-b participated in co-operative binding with β-Pth, whereas the mutant Pin-b did not bind to the lipid layer in the presence of β-Pth. The results provide further insight into the role of hydrophobic and cationic amino acid residues in antimicrobial activity.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > School of Pharmacy > Pharmaceutics Research Group
Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Food and Nutritional Sciences > Food and Bioprocessing Research Group
ID Code:33527
Publisher:American Chemical Society

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