Interaction of wheat α-thionin with large unilamellar vesicles

Jose Manuel Martinez Caaveiro, Antonio Molina, Pablo Rodríguez-Palenzuela, Félix M. Goñi, Juan Manuel González-Mañas

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

The interaction of the wheat antibacterial peptide α-thionin with large unilamellar vesicles has been investigated by means of fluorescence spectroscopy. Binding of the peptide to the vesicles is followed by the release of vesicle contents, vesicle aggregation, and lipid mixing. Vesicle fusion, i.e., mixing of the aqueous contents, was not observed. Peptide binding is governed by electrostatic interactions and shows no cooperativity. The amphipatic nature of wheat α-thionin seems to destabilitize the membrane bilayer and trigger the aggregation of the vesicles and lipid mixing. The presence of distearoylphosphatidylethanolamine-poly(ethylene glycol 2000) (PEG-PE) within the membrane provides a steric barrier that inhibits vesicle aggregation and lipid mixing but does not prevent leakage. Vesicle leakage through discrete membrane channels is unlikely, because the release of encapsulated large fluorescent dextrans is very similar to that of 8- aminonaphthalene-1,3,6,trisulfonic acid (ANTS). A minimum number of 700 peptide molecules must bind to each vesicle to produce complete leakage, which suggests a mechanism in which the overall destabilization of the membrane is due to the formation of transient pores rather than discrete channels.

Original languageEnglish
Pages (from-to)2567-2577
Number of pages11
JournalProtein Science
Volume7
Issue number12
DOIs
Publication statusPublished - Jan 1 1998
Externally publishedYes

Fingerprint

Thionins
Unilamellar Liposomes
Triticum
Peptides
Agglomeration
Membranes
Lipids
1-Naphthylamine
Ethylene Glycol
Fluorescence Spectrometry
Fluorescence spectroscopy
Coulomb interactions
Dextrans
Static Electricity
Ion Channels
Polyethylene glycols
Fusion reactions
Molecules
Acids

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

Cite this

Martinez Caaveiro, J. M., Molina, A., Rodríguez-Palenzuela, P., Goñi, F. M., & González-Mañas, J. M. (1998). Interaction of wheat α-thionin with large unilamellar vesicles. Protein Science, 7(12), 2567-2577. https://doi.org/10.1002/pro.5560071210

Interaction of wheat α-thionin with large unilamellar vesicles. / Martinez Caaveiro, Jose Manuel; Molina, Antonio; Rodríguez-Palenzuela, Pablo; Goñi, Félix M.; González-Mañas, Juan Manuel.

In: Protein Science, Vol. 7, No. 12, 01.01.1998, p. 2567-2577.

Research output: Contribution to journalArticle

Martinez Caaveiro, JM, Molina, A, Rodríguez-Palenzuela, P, Goñi, FM & González-Mañas, JM 1998, 'Interaction of wheat α-thionin with large unilamellar vesicles', Protein Science, vol. 7, no. 12, pp. 2567-2577. https://doi.org/10.1002/pro.5560071210
Martinez Caaveiro JM, Molina A, Rodríguez-Palenzuela P, Goñi FM, González-Mañas JM. Interaction of wheat α-thionin with large unilamellar vesicles. Protein Science. 1998 Jan 1;7(12):2567-2577. https://doi.org/10.1002/pro.5560071210
Martinez Caaveiro, Jose Manuel ; Molina, Antonio ; Rodríguez-Palenzuela, Pablo ; Goñi, Félix M. ; González-Mañas, Juan Manuel. / Interaction of wheat α-thionin with large unilamellar vesicles. In: Protein Science. 1998 ; Vol. 7, No. 12. pp. 2567-2577.
@article{53eac1a1377b4077bab3f640f4d9726b,
title = "Interaction of wheat α-thionin with large unilamellar vesicles",
abstract = "The interaction of the wheat antibacterial peptide α-thionin with large unilamellar vesicles has been investigated by means of fluorescence spectroscopy. Binding of the peptide to the vesicles is followed by the release of vesicle contents, vesicle aggregation, and lipid mixing. Vesicle fusion, i.e., mixing of the aqueous contents, was not observed. Peptide binding is governed by electrostatic interactions and shows no cooperativity. The amphipatic nature of wheat α-thionin seems to destabilitize the membrane bilayer and trigger the aggregation of the vesicles and lipid mixing. The presence of distearoylphosphatidylethanolamine-poly(ethylene glycol 2000) (PEG-PE) within the membrane provides a steric barrier that inhibits vesicle aggregation and lipid mixing but does not prevent leakage. Vesicle leakage through discrete membrane channels is unlikely, because the release of encapsulated large fluorescent dextrans is very similar to that of 8- aminonaphthalene-1,3,6,trisulfonic acid (ANTS). A minimum number of 700 peptide molecules must bind to each vesicle to produce complete leakage, which suggests a mechanism in which the overall destabilization of the membrane is due to the formation of transient pores rather than discrete channels.",
author = "{Martinez Caaveiro}, {Jose Manuel} and Antonio Molina and Pablo Rodr{\'i}guez-Palenzuela and Go{\~n}i, {F{\'e}lix M.} and Gonz{\'a}lez-Ma{\~n}as, {Juan Manuel}",
year = "1998",
month = "1",
day = "1",
doi = "10.1002/pro.5560071210",
language = "English",
volume = "7",
pages = "2567--2577",
journal = "Protein Science",
issn = "0961-8368",
publisher = "Cold Spring Harbor Laboratory Press",
number = "12",

}

TY - JOUR

T1 - Interaction of wheat α-thionin with large unilamellar vesicles

AU - Martinez Caaveiro, Jose Manuel

AU - Molina, Antonio

AU - Rodríguez-Palenzuela, Pablo

AU - Goñi, Félix M.

AU - González-Mañas, Juan Manuel

PY - 1998/1/1

Y1 - 1998/1/1

N2 - The interaction of the wheat antibacterial peptide α-thionin with large unilamellar vesicles has been investigated by means of fluorescence spectroscopy. Binding of the peptide to the vesicles is followed by the release of vesicle contents, vesicle aggregation, and lipid mixing. Vesicle fusion, i.e., mixing of the aqueous contents, was not observed. Peptide binding is governed by electrostatic interactions and shows no cooperativity. The amphipatic nature of wheat α-thionin seems to destabilitize the membrane bilayer and trigger the aggregation of the vesicles and lipid mixing. The presence of distearoylphosphatidylethanolamine-poly(ethylene glycol 2000) (PEG-PE) within the membrane provides a steric barrier that inhibits vesicle aggregation and lipid mixing but does not prevent leakage. Vesicle leakage through discrete membrane channels is unlikely, because the release of encapsulated large fluorescent dextrans is very similar to that of 8- aminonaphthalene-1,3,6,trisulfonic acid (ANTS). A minimum number of 700 peptide molecules must bind to each vesicle to produce complete leakage, which suggests a mechanism in which the overall destabilization of the membrane is due to the formation of transient pores rather than discrete channels.

AB - The interaction of the wheat antibacterial peptide α-thionin with large unilamellar vesicles has been investigated by means of fluorescence spectroscopy. Binding of the peptide to the vesicles is followed by the release of vesicle contents, vesicle aggregation, and lipid mixing. Vesicle fusion, i.e., mixing of the aqueous contents, was not observed. Peptide binding is governed by electrostatic interactions and shows no cooperativity. The amphipatic nature of wheat α-thionin seems to destabilitize the membrane bilayer and trigger the aggregation of the vesicles and lipid mixing. The presence of distearoylphosphatidylethanolamine-poly(ethylene glycol 2000) (PEG-PE) within the membrane provides a steric barrier that inhibits vesicle aggregation and lipid mixing but does not prevent leakage. Vesicle leakage through discrete membrane channels is unlikely, because the release of encapsulated large fluorescent dextrans is very similar to that of 8- aminonaphthalene-1,3,6,trisulfonic acid (ANTS). A minimum number of 700 peptide molecules must bind to each vesicle to produce complete leakage, which suggests a mechanism in which the overall destabilization of the membrane is due to the formation of transient pores rather than discrete channels.

UR - http://www.scopus.com/inward/record.url?scp=0031700044&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031700044&partnerID=8YFLogxK

U2 - 10.1002/pro.5560071210

DO - 10.1002/pro.5560071210

M3 - Article

C2 - 9865951

AN - SCOPUS:0031700044

VL - 7

SP - 2567

EP - 2577

JO - Protein Science

JF - Protein Science

SN - 0961-8368

IS - 12

ER -