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Raman Study of the Puroindoline-a/Lysopamitoylphosphatidylcholine Interaction in Free Standing Black Films

hal.structure.identifierCentre de physique moléculaire optique et hertzienne [CPMOH]
dc.contributor.authorSANDRAS, Florent
hal.structure.identifierCentre de Recherche en Sciences et Ingénierie des Macromolécules
dc.contributor.authorPÉZOLET, Michel
hal.structure.identifierUnité de recherche sur les Biopolymères, Interactions Assemblages [BIA]
dc.contributor.authorMARION, Didier
hal.structure.identifierCentre de physique moléculaire optique et hertzienne [CPMOH]
dc.contributor.authorGRAUBY-HEYWANG, Christine
dc.date.created2009-02-10
dc.date.issued2009-07-21
dc.identifier.issn0743-7463
dc.description.abstractEnThe conformation of puroindoline-a (PIN-a), a protein extracted from wheat endosperm, in free-standing black films has been studied using confocal Raman spectroscopy. This protein is characterized by the presence in its sequence of a unique tryptophan (Trp)-rich domain and of five disulfide bridges stabilizing its three-dimensional structure. PIN-a is able to form free-standing films, which are very stable in time, because of its remarkable surface-active properties. These films become black in a few hours and are characterized by the presence of numerous aggregates. Their Raman spectra show major modifications or the PIN-a structure as compared to the solid form, such as the formation of beta-sheets or unordered structures, the modification of the environment of the Trp domain and, the conformation of disulfide bridges. These modifications are in agreement with an unfolding of the protein at the interfaces of the film and suggest that the Trp domain is involved in the aggregation. We have also studied the influence of increasing amounts of lysopalmitoylphosphatidylcholine (LPC) into the films. The direct observation of these mixed films shows that LPC inhibits the formation of PIN-a aggregates and that the conformation of PIN-a is strongly correlated to the LPC/PIN-a molar ratio. Raman spectroscopy also shows that PIN-a disturbs the highly organized arrangement of LPC molecules in the film.
dc.language.isoen
dc.publisherAmerican Chemical Society
dc.title.enRaman Study of the Puroindoline-a/Lysopamitoylphosphatidylcholine Interaction in Free Standing Black Films
dc.typeArticle de revue
dc.identifier.doi10.1021/la9005086
dc.subject.halSciences du Vivant [q-bio]/Ingénierie des aliments
dc.subject.halSciences de l'ingénieur [physics]/Génie des procédés
bordeaux.journalLangmuir
bordeaux.page8181-8186
bordeaux.volume25
bordeaux.issue14
bordeaux.peerReviewedoui
hal.identifierhal-00670472
hal.version1
hal.popularnon
hal.audienceInternationale
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-00670472v1
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