Fiche publication
Date publication
juillet 2018
Journal
Biomacromolecules
Auteurs
Membres identifiés du Cancéropôle Est :
Dr FRISCH Benoit
,
Pr SCHAAF Pierre
Tous les auteurs :
Bergthold C, Hauser D, Chaumont A, El Yakhlifi S, Mateescu M, Meyer F, Metz-Boutigue MH, Frisch B, Schaaf P, Ihiawakrim D, Ersen O, Monnier CA, Petri-Fink A, Rothen-Rutishauser B, Ball V
Lien Pubmed
Résumé
The oxidation of dopamine and of other catecholamines leads to the formation of conformal films on the surface of all known materials and to the formation of a precipitate in solution. In some cases, it has been shown that the addition of additives in the dopamine solution, like certain surfactants or polymers, polyelectrolytes and certain proteins allow to get polydopamine nanoparticles of controlled size and the concomitant decrease, in an additive/dopamine dependent manner, in film formation on the surface of the reaction beaker. However, the mechanism behind this controlled oxidation and self-assembly of catecholamines is not known. In this article, it is shown that a specific diad of amino acids in proteins, namely KE, allows for specific control in the oxidation-self assembly of dopamine to obtain polydopamine@protein core shell nanoparticles which are biocompatible. The interactions between dopamine and the adjacent KE amino acids potentially responsible for the size control of polydopamine aggregates was investigated by molecular dynamics simulations. The obtained core-shell nanoparticles display the biological activity of the protein used to control the self-assembly of PDA. The photon to heat conversion ability of PDA is conserved in the PDA@protein particles.
Référence
Biomacromolecules. 2018 Jul 30;:
