Structure of proteins under pressure: Covalent binding effects of biliverdin on β-lactoglobulin - Archive ouverte HAL Access content directly
Journal Articles Biophysical Journal Year : 2022

Structure of proteins under pressure: Covalent binding effects of biliverdin on β-lactoglobulin

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Abstract

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.
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Dates and versions

hal-03861780 , version 1 (20-11-2022)

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Simeon Minić, Burkhard Annighöfer, Arnaud Hélary, Laïla Sago, David Cornu, et al.. Structure of proteins under pressure: Covalent binding effects of biliverdin on β-lactoglobulin. Biophysical Journal, 2022, 121 (13), pp.2514-2525. ⟨10.1016/j.bpj.2022.06.003⟩. ⟨hal-03861780⟩
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