Investigation at residue level of the early steps during the assembly of two proteins into supramolecular objects.

D.B. Salvatore N. Duraffourg A. Favier B.A. Persson M. Lund M.M. Delage R. Silvers H. Schwalbe Thomas Croguennec 1 S. Bouhallab V. Forge
1 STLO - Science et Technologie du Lait et de l'Oeuf
Abstract : Understanding the driving forces governing protein assembly requires the characterization of interactions at molecular level. We focus on two homologous oppositely charged proteins, lysozyme and α-lactalbumin, which can assemble into microspheres. The assembly early steps were characterized through the identification of interacting surfaces monitored at residue level by NMR chemical shift perturbations by titrating one (15)N-labeled protein with its unlabeled partner. While α-lactalbumin has a narrow interacting site, lysozyme has interacting sites scattered on a broad surface. The further assembly of these rather unspecific heterodimers into tetramers leads to the establishment of well-defined interaction sites. Within the tetramers, most of the electrostatic charge patches on the protein surfaces are shielded. Then, hydrophobic interactions, which are possible because α-lactalbumin is in a partially folded state, become preponderant, leading to the formation of larger oligomers. This approach will be particularly useful for rationalizing the design of protein assemblies as nanoscale devices.
Keywords : bovine alpha-lactalbumin molten globule state egg-white lysozyme nmr-spectroscopy phosphotransferase system beta-lactoglobulin amyloid fibrils metal-ions binding aggregation
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Article dans une revue
Biomacromolecules, American Chemical Society, 2011, 12 (6), pp.2200-10. 〈10.1021/bm200285e〉
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https://hal-agrocampus-ouest.archives-ouvertes.fr/hal-00729257
Contributeur : Céline Martel <>
Soumis le : vendredi 7 septembre 2012 - 15:30:52
Dernière modification le : mercredi 21 mars 2018 - 16:08:07

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AGROCAMPUS-OUEST | UNAM | INRA | AGROCAMPUS-OUEST-UMR-STLO

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D.B. Salvatore, N. Duraffourg, A. Favier, B.A. Persson, M. Lund, et al.. Investigation at residue level of the early steps during the assembly of two proteins into supramolecular objects.. Biomacromolecules, American Chemical Society, 2011, 12 (6), pp.2200-10. 〈10.1021/bm200285e〉. 〈hal-00729257〉

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