Laboratoire Léon Brillouin
UMR12 CEA-CNRS, Bât. 563 CEA Saclay
91191 Gif sur Yvette Cedex, France
Simeon Minić, Burkhard Annighöfer, Arnaud Hélary, Laïla Sago, David Cornu, Annie Brûlet, Sophie Combet
High pressure (HP) is a particularly powerful tool to study protein folding/unfolding, revealing subtle structural rearrangements. Bovine β-lactoglobulin (BLG), a protein of interest in food science, exhibits a strong propensity to bind various bioactive molecules. We probed the effects of the binding of biliverdin (BV), a tetrapyrrole linear chromophore, on the stability of BLG under pressure, by combining in situ HP small-angle neutron scattering (SANS) and HP-UV absorption spectroscopy. Although BV induces a slight destabilization of BLG during HP-induced unfolding, a ligand excess strongly prevents BLG oligomerization. Moreover, at SANS resolution, an excess of BV induces the complete recovery of the protein “native” 3D structure after HP removal, despite the presence of the BV covalently bound adduct. Mass spectrometry highlights the crucial role of cysteine residues in the competitive and protective effects of BV during pressure denaturation of BLG through SH/S-S exchange.
A presentation in French on Scoop.it! of the Paris-Saclay University.
• Physics and chemistry for life sciences and the environment › Physics and life Physique et chimie pour le vivant et l’environnement
• Laboratoire Léon Brillouin (LLB) • Leon Brillouin Laboratory (LLB)
• Groupe "Matière molle et biophysique" - MMB • Small angle scattering
• Neutrons • Activités instrumentales nationales et internationales du LLB - National and internatonial instrumental activities at the LLB • Neutrons • Small Angle Neutron Scattering (PA)