This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Dubreil, L. Articles by Renault, A. Search for Related Content PubMed PubMed Citation Articles by Dubreil, L. Articles by Renault, A.

Aggregation of Puroindoline in Phospholipid Monolayers Spread at the Air-Liquid Interface

L. Dubreil ^*, V. Vié ^*, S. Beaufils ^*, D. Marion  and A. Renault ^*

^* Groupe Matière Condensée et Matériaux, Université de Rennes, Campus Beaulieu, Rennes, France; and Unité de Recherche sur les Protéines Végétales et leurs Interactions, Institut National de la Recherche Agronomique, Nantes, France

Correspondence: Address reprint requests to Laurence Dubreil, Institut National de la Recherche sur les Protéines Végétales et Leurs Interactions, rue de la Géraudière, B.P. 71 627, F-44316 Nantes Cedex 3. Tel.: 33-024-067-50-56; Fax: 33-024-067-50-25; E-mail: laurence.dubreil{at}wanadoo.fr.

Puroindolines, cationic and cystine-rich low molecular weight lipid binding proteins from wheat seeds, display unique foaming properties and antimicrobial activity. To unravel the mechanism involved in these properties, the interaction of puroindoline-a (PIN-a) with dipalmitoylphosphatidylcholine (DPPC) and dipalmitoylphosphatidylglycerol (DPPG) monolayers was studied by coupling Langmuir-Blodgett and imaging techniques. Compression isotherms of PIN-a/phospholipid monolayers and adsorption of PIN-a to lipid monolayers showed that the protein interacted strongly with phospholipids, especially with the anionic DPPG. The electrostatic contribution led to the formation of a highly stable lipoprotein monolayer. Confocal laser scanning microscopy and atomic force microscopy showed that PIN-a was mainly inserted in the liquid-expanded phase of the DPPC, where it formed an aggregated protein network and induced the fusion of liquid-condensed domains. For DPPG, the protein partitioned in both the liquid-expanded and liquid-condensed phases, where it was aggregated. The extent of protein aggregation was related both to the physical state of phospholipids, i.e., condensed or expanded, and to the electrostatic interactions between lipids and PIN-a. Aggregation of PIN-a at air-liquid and lipid interfaces could account for the biological and technological properties of this wheat lipid binding protein.

This article has been cited by other articles:

				S. L. Duncan and R. G. Larson Comparing Experimental and Simulated Pressure-Area Isotherms for DPPC Biophys. J., April 15, 2008; 94(8): 2965 - 2986. [Abstract] [Full Text] [PDF]

				M. D. Lad, F. Birembaut, L. A. Clifton, R. A. Frazier, J. R. P. Webster, and R. J. Green Antimicrobial Peptide-Lipid Binding Interactions and Binding Selectivity Biophys. J., May 15, 2007; 92(10): 3575 - 3586. [Abstract] [Full Text] [PDF]

				F. Neville, M. Cahuzac, O. Konovalov, Y. Ishitsuka, K. Y. C. Lee, I. Kuzmenko, G. M. Kale, and D. Gidalevitz Lipid Headgroup Discrimination by Antimicrobial Peptide LL-37: Insight into Mechanism of Action Biophys. J., February 15, 2006; 90(4): 1275 - 1287. [Abstract] [Full Text] [PDF]

				V. M. Bolanos-Garcia, S. Beaufils, A. Renault, J. G. Grossmann, S. Brewerton, M. Lee, A. Venkitaraman, and T. L. Blundell The Conserved N-Terminal Region of the Mitotic Checkpoint Protein BUBR1: A Putative TPR Motif of High Surface Activity Biophys. J., October 1, 2005; 89(4): 2640 - 2649. [Abstract] [Full Text] [PDF]