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Full Record Details
Persistent URL
http://purl.org/net/epubs/work/65838
Record Status
Checked
Record Id
65838
Title
Selected Wheat Seed Defense Proteins Exhibit Competitive Binding to Model Microbial Lipid Interfaces
Contributors
MR Sanders
,
LA Clifton (STFC Rutherford Appleton Lab.)
,
C Neylon (STFC Rutherford Appleton Lab.)
,
RA Frazier
,
RJ Green
Abstract
Puroindolines (Pins) and purothionins (Pths) are basic, amphiphilic, cysteine-rich wheat proteins that play a role in plant defense against microbial pathogens. This study 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.
Organisation
ISIS
,
ISIS-CRISP
,
ISIS-SURF
,
STFC
Keywords
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Language
English (EN)
Type
Details
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Year
Journal Article
Journal of Agricultural and Food Chemistry 61, no. 28 (2013): 6890-6900.
doi:10.1021/jf401336a
2013
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