Rubber particle proteins REF1 and SRPP1 interact differently with native lipids extracted from Hevea brasiliensis latex
BERTHELOT, Karine
Chimie et Biologie des Membranes et des Nanoobjets [CBMN]
Laboratoire de Chimie des Polymères Organiques [LCPO]
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Chimie et Biologie des Membranes et des Nanoobjets [CBMN]
Laboratoire de Chimie des Polymères Organiques [LCPO]
BERTHELOT, Karine
Chimie et Biologie des Membranes et des Nanoobjets [CBMN]
Laboratoire de Chimie des Polymères Organiques [LCPO]
Chimie et Biologie des Membranes et des Nanoobjets [CBMN]
Laboratoire de Chimie des Polymères Organiques [LCPO]
PERUCH, Frédéric
Laboratoire de Chimie des Polymères Organiques [LCPO]
Team 1 LCPO : Polymerization Catalyses & Engineering
< Reduce
Laboratoire de Chimie des Polymères Organiques [LCPO]
Team 1 LCPO : Polymerization Catalyses & Engineering
Language
en
Article de revue
This item was published in
Biochimica et Biophysica Acta:Biomembranes. 2017, vol. 1859, n° 2, p. 201-210
Elsevier
English Abstract
Rubber 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 ...Read more >
Rubber 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 PL, GL or NL, without modification of its structure. In contrast REF1 inserts deeply in the lipid monolayers with all lipid classes. With NL, REF1 is even able to switch from α-helice conformation to β-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 particlesRead less <
English Keywords
Hevea brasiliensis rubber particle proteins
Langmuir monolayer
Latex native lipids
Polarization modulated-infrared reflection absorption spectroscopy
Rubber elongation factor
Small rubber particle protein
ANR Project
ANR-10-CD2I-08 - null
De 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-CE07-0026
De 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-CE07-0026
Origin
Hal imported