The role of protein hydrophobicity in thionin-phospholipid interactions : A comparison of α1 and α2-purothionin adsorbed anionic phospholipid monolayers
Clifton, Luke A. ; Sanders, Michael ; Kinane, Christian ; Arnold, Tom ; Edler, Karen J. LU
; Neylon, Cameron
; Green, Rebecca J.
and Frazier, Richard A.
(2012)
In Physical Chemistry Chemical Physics
14(39).
p.13569-13579
- Abstract
The plant defence proteins α1- and α2-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 α1- and α2-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 α1 and α2-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... (More)
The plant defence proteins α1- and α2-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 α1- and α2-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 α1 and α2-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 α2-Pth showed faster disruption of the lipid film and removed more phospholipid (12%) from the interface than α1-Pth. Correlating the protein properties and lipid binding activity suggests that hydrophobicity plays a key role in the membrane lipid removal activity of thionins.
(Less)
- author
- Clifton, Luke A.
; Sanders, Michael
; Kinane, Christian
; Arnold, Tom
; Edler, Karen J.
LU
; Neylon, Cameron
; Green, Rebecca J.
and Frazier, Richard A.
- publishing date
- 2012-10-21
- type
- Contribution to journal
- publication status
- published
- in
- Physical Chemistry Chemical Physics
- volume
- 14
- issue
- 39
- pages
- 11 pages
- publisher
- Royal Society of Chemistry
- external identifiers
-
- pmid:22955734
- scopus:84866648692
- ISSN
- 1463-9076
- DOI
- 10.1039/c2cp42029e
- language
- English
- LU publication?
- no
- id
- 6cb78213-775d-497e-96b0-8b3f1db2ff54
- date added to LUP
- 2023-05-04 18:39:15
- date last changed
- 2025-10-14 11:58:23
@article{6cb78213-775d-497e-96b0-8b3f1db2ff54,
abstract = {{<p>The plant defence proteins α1- and α2-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 α1- and α2-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 α1 and α2-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 α2-Pth showed faster disruption of the lipid film and removed more phospholipid (12%) from the interface than α1-Pth. Correlating the protein properties and lipid binding activity suggests that hydrophobicity plays a key role in the membrane lipid removal activity of thionins.</p>}},
author = {{Clifton, Luke A. and Sanders, Michael and Kinane, Christian and Arnold, Tom and Edler, Karen J. and Neylon, Cameron and Green, Rebecca J. and Frazier, Richard A.}},
issn = {{1463-9076}},
language = {{eng}},
month = {{10}},
number = {{39}},
pages = {{13569--13579}},
publisher = {{Royal Society of Chemistry}},
series = {{Physical Chemistry Chemical Physics}},
title = {{The role of protein hydrophobicity in thionin-phospholipid interactions : A comparison of α1 and α2-purothionin adsorbed anionic phospholipid monolayers}},
url = {{http://dx.doi.org/10.1039/c2cp42029e}},
doi = {{10.1039/c2cp42029e}},
volume = {{14}},
year = {{2012}},
}