Fiche publication
Date publication
janvier 2024
Journal
International journal of biological macromolecules
Auteurs
Membres identifiés du Cancéropôle Est :
Dr MAURIZI Lionel
Tous les auteurs :
Marques C, Maroni P, Maurizi L, Jordan O, Borchard G
Lien Pubmed
Résumé
Nanoparticles (NPs) in contact with biological fluids form a biomolecular corona through interactions with proteins, lipids, and sugars, acquiring new physicochemical properties. This work explores the interaction between selected proteins (hemoglobin and fetuin-A) that may alter NP circulation time and NPs of different surface charges (neutral, positive, and negative). The interaction with key proteins albumin and transferrin, the two of the most abundant proteins in plasma was also studied. Binding affinity was investigated using quartz crystal microbalance and fluorescence quenching, while circular dichroism assessed potential conformational changes. The data obtained from in vitro experiments were compared to in vivo protein corona data. The results indicate that electrostatic interactions primarily drive protein-NP interactions, and higher binding affinity does not necessarily translate into more significant structural changes. In vitro and single protein-NP studies provide valuable insights that can be correlated with in vivo observations, opening exciting possibilities for future protein corona studies.
Mots clés
Binding affinity, Conformational changes, Nanoparticle, Protein corona, Protein structure
Référence
Int J Biol Macromol. 2024 01;256(Pt 1):128339