AEM
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Gaussier, H.
Right arrow Articles by Subirade, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Gaussier, H.
Right arrow Articles by Subirade, M.
Agricola
Right arrow Articles by Gaussier, H.
Right arrow Articles by Subirade, M.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, November 2003, p. 6777-6784, Vol. 69, No. 11
0099-2240/03/$08.00+0     DOI: 10.1128/AEM.69.11.6777-6784.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Binding of Pediocin PA-1 with Anionic Lipid Induces Model Membrane Destabilization

Hélène Gaussier, Thierry Lefèvre, and Muriel Subirade*

Chaire de recherche du Canada sur les protéines et les aliments fonctionnels, Centre de recherche en Sciences et Technologie du Lait (STELA), and Institut sur les nutraceutiques et aliments fonctionnels (INAF), Département des sciences des aliments et de nutrition, Université Laval, Pavillon Paul-Comtois, Sainte-Foy, Québec G1K 7P4, Canada

Received 6 May 2003/ Accepted 19 August 2003

To obtain molecular insights into the action mode of antimicrobial activity of pediocin PA-1, the interactions between this bacteriocin and dimyristoylphosphatidylcholine (DMPC) or dimyristoylphosphatidylglycerol (DMPG) model membranes have been investigated in D2O at pD 6 by Fourier transform infrared spectroscopy. The interactions were monitored with respect to alteration of the secondary structure of pediocin, as registered by the amide I' band, and phospholipid conformation, as revealed by the methylene {nu}s(CH2) and carbonyl {nu}(C;O) stretching vibrations. The results show that no interaction between pediocin and DMPC occurs. By contrast, pediocin undergoes a structural reorganization in the presence of DMPG. Upon heating, pediocin self-aggregates, which is not observed for this pD in aqueous solution. The gel-to-crystalline phase transition of DMPG shifts to higher temperatures with a concomitant dehydration of the interfacial region. Our results indicate that pediocin is an extrinsic peptide and that its action mechanism may lie in a destabilization of the cell membrane.

* Corresponding author. Mailing address: Chaire de recherche du Canada sur les protéines et les aliments fonctionnels, Centre de recherche en Sciences et Technologie du Lait (STELA), et Institut sur les nutraceutiques et aliments fonctionnels (INAF), Université Laval, Département des sciences des aliments et de nutrition, Pavillon Paul-Comtois, Sainte-Foy, Québec G1K 7P4, Canada. Phone: (418) 656-4278. Fax: (418) 656-3353. E-mail: Muriel.subirade{at}aln.ulaval.ca.

Applied and Environmental Microbiology, November 2003, p. 6777-6784, Vol. 69, No. 11
0099-2240/03/$08.00+0     DOI: 10.1128/AEM.69.11.6777-6784.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.





Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. Microbiol. Mol. Biol. Rev. Eukaryot. Cell All ASM Journals

Copyright © 2003 by the American Society for Microbiology. All rights reserved.