Fiche publication
Date publication
septembre 2021
Journal
Langmuir : the ACS journal of surfaces and colloids
Auteurs
Membres identifiés du Cancéropôle Est :
Dr LAVALLE Philippe
Tous les auteurs :
Touzeau J, Seydou M, Maurel F, Tallet L, Mutschler A, Lavalle P, Barbault F
Lien Pubmed
Résumé
Inorganic materials used for biomedical applications such as implants generally induce the adsorption of proteins on their surface. To control this phenomenon, the bioinspired peptidomimetic polymer 1 (PMP1), which aims to reproduce the adhesion of mussel foot proteins, is commonly used to graft specific proteins on various surfaces and to regulate the interfacial mechanism. To date and despite its wide application, the elucidation at the atomic scale of the PMP1 mechanism of adsorption on surfaces is still unknown. The purpose of the present work was thus to unravel this process through experimental and computational investigations of adsorption of PMP1 on gold, TiO, and SiO surfaces. A common mechanism of adsorption is identified for the adsorption of PMP1 which emphasizes the role of electrostatics to approach the peptide onto the surface followed by a full adhesion process where the entropic desolvation step plays a key role. Besides, according to the fact that mussel naturally controls the oxidation states of its proteins, further investigations were performed for two distinct redox states of PMP1, and we conclude that even if both states are able to allow interaction of PMP1 with the surfaces, the oxidation of PMP1 leads to a stronger interaction.
Référence
Langmuir. 2021 Sep 13;:
