Control of Surface-Localized, Enzyme-Assisted Self-Assembly of Peptides through Catalyzed Oligomerization.
Fiche publication
Date publication
août 2017
Journal
Langmuir : the ACS journal of surfaces and colloids
Auteurs
Membres identifiés du Cancéropôle Est :
Pr SCHAAF Pierre, Dr SCHMUTZ Marc
Tous les auteurs :
Vigier-Carrière C, Wagner D, Chaumont A, Durr B, Lupattelli P, Lambour C, Schmutz M, Hemmerlé J, Senger B, Schaaf P, Boulmedais F, Jierry L
Lien Pubmed
Résumé
Localized self-assembly allowing both spatial and temporal control over the assembly process is essential in many biological systems. This can be achieved through localized enzyme-assisted self-assembly (LEASA), also called enzyme-instructed self-assembly, where enzymes present on a substrate catalyze a reaction that transforms noninteracting species into self-assembling ones. Very few LEASA systems have been reported so far, and the control of the self-assembly process through the surface properties represents one essential step toward their use, for example, in artificial cell mimicry. Here, we describe a new type of LEASA system based on α-chymotrypsin adsorbed on a surface, which catalyzes the production of (KL)OEt oligopeptides from a KLOEt (K: lysine; L: leucine; OEt ethyl ester) solution. When a critical concentration of the formed oligopeptides is reached near the surface, they self-assemble into β-sheets resulting in a fibrillar network localized at the interface that can extend over several micrometers. One significant feature of this process is the existence of a lag time before the self-assembly process starts. We investigate, in particular, the effect of the α-chymotrypsin surface density and KLOEt concentration on the self-assembly kinetics. We find that the lag time can be finely tuned through the surface density in α-chymotrypsin and KLOEt concentration. For a given surface enzyme concentration, a critical KLOEt concentration exists below which no self-assembly takes place. This concentration increases when the surface density in enzyme decreases.
Mots clés
Kinetics, Oligopeptides, Peptides, chemistry, Surface Properties
Référence
Langmuir. 2017 08 22;33(33):8267-8276