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dc.rights.licenseopenen_US
dc.contributor.authorWADEESIRISAK, Kanthida
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorCASTANO, Sabine
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorBERTHELOT, Karine
dc.contributor.authorVAYSSE, Laurent
dc.contributor.authorBONFILS, Frederic
hal.structure.identifierTeam 1 LCPO : Polymerization Catalyses & Engineering
dc.contributor.authorPERUCH, Frederic
dc.contributor.authorRATTANAPORN, Kittipong
dc.contributor.authorLIENGPRAYOON, Siriluck
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorLECOMTE, Sophie
dc.contributor.authorBOTTIER, Celine
dc.date.accessioned2021-07-12T15:28:15Z
dc.date.available2021-07-12T15:28:15Z
dc.date.issued2017-02
dc.identifier.issn0005-2736en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/106530
dc.description.abstractEnRubber particle membranes from the Hevea latex contain predominantly two proteins, REF1 and SRPP1 involved in poly(cis-1,4-isoprene) synthesis or rubber quality. The repartition of both proteins on the small or large rubber particles seems to differ, but their role in the irreversible coagulation of the rubber particle is still unknown. In this study we highlighted the different modes of interactions of both recombinant proteins with different classes of lipids extracted from Hevea brasiliensis latex, and defined as phospholipids (PL), glycolipids (GL) and neutral lipids (NL). We combined two biophysical methods, polarization modulated-infrared reflection adsorption spectroscopy (PM-IRRAS) and ellipsometry to elucidate their interactions with monolayers of each class of lipids. REF1 and SRPP1 interactions with native lipids are clearly different; SRPP1 interacts mostly in surface with PI, GL or NL, without modification of its structure. In contrast REF1 inserts deeply in the lipid monolayers with all lipid classes. With NI, REF1 is even able to switch from alpha-helice conformation to beta-sheet structure, as in its aggregated form (amyloid form). Interaction between REF1 and NL may therefore have a specific role in the irreversible coagulation of rubber particles.
dc.description.sponsorshipANR-10-CD2I-08en_US
dc.description.sponsorshipDe la particule de caoutchouc d'hévéa à la structure et aux propriétés du caoutchouc naturel: vers l'optimisation des performances du caoutchouc naturel - ANR-14-CE07-0026en_US
dc.language.isoENen_US
dc.subject.enHevea brasiliensis rubber particle proteins
dc.subject.enRubber elongation factor
dc.subject.enSmall rubber particle protein
dc.subject.enLatex native lipids
dc.subject.enLangmuir monolayer
dc.subject.enPolarization modulated-infrared reflection absorption spectroscopy
dc.title.enRubber particle proteins REF1 and SRPP1 interact differently with native lipids extracted from Hevea brasiliensis latex
dc.typeArticle de revueen_US
dc.identifier.doi10.1016/j.bbamem.2016.11.010en_US
dc.subject.halChimie/Matériauxen_US
bordeaux.journalBiochimica Et Biophysica Acta-Biomembranesen_US
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248en_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionCNRS
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
hal.identifierhal-01473711
hal.exportfalse
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