Issue 38, 2011
From the journal:

Physical Chemistry Chemical Physics

Lipid binding interactions of antimicrobial plant seed defence proteins: puroindoline-a and β-purothionin†

Luke A. Clifton,a   Michael R. Sanders,bc   Arwel V. Hughes,a   Cameron Neylon,a   Richard A. Frazierb  and  Rebecca J. Greenc  

a ISIS Spallation Neutron Source, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Harwell Science and Innovation Campus, Didcot, Oxfordshire, UK
E-mail: luke.clifton@stfc.ac.uk

b Department of Food and Nutritional Sciences, University of Reading, PO Box 226, Whiteknights, Reading, UK
E-mail: r.a.frazier@reading.ac.uk

c Reading School of Pharmacy, University of Reading, PO Box 226, Whiteknights, Reading, UK
E-mail: rebecca.green@reading.ac.uk

Abstract

The indolines and thionins are basic, amphiphilic and cysteine-rich proteins found in cereals; puroindoline-a (Pin-a) and β-purothionin (β-Pth) are members of these families in wheat (Triticum aestivum). Pin-a and β-Pth have been suggested to play a significant role in seed defence against microbial pathogens, making the interaction of these proteins with model bacterial membranes an area of potential interest. We have examined the binding of these proteins to lipid monolayers composed of 1,2-dipalmitoyl-sn-glycero-3-phospho-(1′-rac-glycerol) (DPPG) using a combination of neutron reflectometry, Brewster angle microscopy, and infrared spectroscopy. Results showed that both Pin-a and β-Pth interact strongly with condensed phase DPPG monolayers, but the degree of penetration was different. β-Pth was shown to penetrate the lipid acyl chain region of the monolayer and remove lipids from the air/liquid interface during the adsorption process, suggesting this protein may be able to both form membrane spanning ion channels and remove membrane phospholipids in its lytic activity. Conversely, Pin-a was shown to interact mainly with the head-group region of the condensed phase DPPG monolayer and form a 33 Å thick layer below the lipid film. The differences between the interfacial structures formed by these two proteins may be related to the differing composition of the Pin-a and β-Pth hydrophobic regions.

Graphical abstract: Lipid binding interactions of antimicrobial plant seed defence proteins: puroindoline-a and β-purothionin

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Article information

DOI
https://doi.org/10.1039/C1CP21799B
Article type
Paper
Submitted
02 Jun 2011
Accepted
10 Aug 2011
First published
25 Aug 2011

Phys. Chem. Chem. Phys., 2011,13, 17153-17162

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Lipid binding interactions of antimicrobial plant seed defence proteins: puroindoline-a and β-purothionin

L. A. Clifton, M. R. Sanders, A. V. Hughes, C. Neylon, R. A. Frazier and R. J. Green, Phys. Chem. Chem. Phys., 2011, 13, 17153 DOI: 10.1039/C1CP21799B

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