GALLUZZI, Francesca; CHAIGNEPAIN, Stephane; ARSLANOGLU, Julie; TOKARSKI, Caroline

doi:10.1016/j.bpc.2022.106861

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GALLUZZI, Francesca

Chimie et Biologie des Membranes et des Nanoobjets [CBMN]

CHAIGNEPAIN, Stephane
Chimie et Biologie des Membranes et des Nanoobjets [CBMN]

ARSLANOGLU, Julie

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Article de revue

Ce document a été publié dans

Biophysical Chemistry. 2022-10-01, vol. 289

Résumé en anglais

Little is known about structural alterations of proteins within the polymeric films of paints. For the first time, hydrogen‑deuterium exchange mass spectrometry (HDX-MS) was implemented to explore the conformational alterations of proteins resulting from their interaction with inorganic pigments within the early stages of the paint film formation. Intact protein analysis and bottom-up electrospray-ionisation mass spectrometry strategies combined with progressively increasing deuterium incubation times were used to compare the protein structures of the model protein hen egg-white lysozyme (HEWL) extracted from newly dried non-pigmented films and newly dried films made from a freshly made mixture of HEWL with lead white pigment (2PbCO3 Pb(OH)2). The action of other pigments was also investigated, expanding the HDX study with a global approach to paint models of HEWL mixed with zinc white (ZnO), cinnabar (HgS) and red lead (Pb3O4) pigments. The results show structural modifications of HEWL induced by the interaction with the pigment metal ions during the paint formulation after drying and prior to ageing. Both the charge distribution of HEWL proteoforms, its oxidation rate and its deuterium absorption rate, were influenced by the pigment type, providing the first insights into the correlation of pigment type/metal cation to specific chemistries related to protein stability.< Réduire

URI

https://oskar-bordeaux.fr/handle/20.500.12278/173044

DOI

http://dx.doi.org/10.1016/j.bpc.2022.106861

Projet Européen

Horizon 2020 Marie Skłodowska-Curie Actions Innovative Training Network (H2020 MSCA-60 ITN)

Unités de recherche

CBMN : Chimie & de Biologie des Membranes & des Nano-objets - UMR 5248