Transition from continuous to microglobular shaped peptide assemblies through a Liesegang-like enzyme-assisted mechanism.

Date publication

novembre 2022

Journal

Journal of colloid and interface science

Auteurs

Membres identifiés du Cancéropôle Est :
Pr SCHAAF Pierre

Tous les auteurs :
Runser JY, Fneich F, Senger B, Weiss P, Jierry L, Schaaf P

Lien Pubmed

https://www.ncbi.nlm.nih.gov/pubmed/36495809

Résumé

Enzyme-assisted self-assembly confined within host materials leads to Liesegang-like spatial structuration when precursor peptides are diffusing through an enzyme-functionalized hydrogel. It is shown here that playing on peptide and enzyme concentrations results in a transition from continuous self-assembled peptide areas to individual microglobules. Their morphology, location, size and buildup mechanism are described. Additionally, it is also found that the enzymes adsorb onto the peptide self-assemblies leading to co-localization of peptide self-assembled microglobules and enzymes. Finally, we find that large microglobules grow at the expense of smaller ones present in their vicinity in a kind of Ostwald ripening process, illustrating the dynamic nature of the peptide self-assembly process within host hydrogels.

Référence

J Colloid Interface Sci. 2022 11 18;633:876-885