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    Control of Surface-Localized, Enzyme-Assisted Self-Assembly of Peptides through Catalyzed Oligomerization

    Year: 2017

    Journal: Langmuir, Volume 33, AUG 22, page 8267–8276

    Authors: Vigier-Carriere, Cecile; Wagner, Deborah; Chaumont, Alain; Durr, Baptiste; Lupattelli, Paolo; Lambour, Christophe; Schmutz, Marc; Hemmerle, Joseph; Senger, Bernard; Schaaf, Pierre; Boulmedais, Fouzia; Jierry, Loic

    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 alpha-chymotrypsin adsorbed on a surface, which catalyzes the production of (KL)(n)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 beta-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 alpha-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 alpha-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.
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