Accelerated hydrolysis of esters catalyzed by receptors, I nonenzymatic cleavage ofp-nitrophenyl acetate by polypeptides

Ryu, Hyeong-Won; Cho, Young; Ko, Thong-Sung

doi:10.1007/bf02475318

Cited by 1 publication

(1 citation statement)

References 13 publications

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“…To circumvent this issue, we used the nucleophilic property of (KL) n OEt oligomers to indirectly follow the growth kinetic of the hydrogel self-assembly. Indeed, as with lysine-rich peptides, we found that the presence of KL 6 in solution triggers the transformation of p-NPA into p-NP (Figure S-7 in the SI). This reaction was used as sensor for the presence of (KL) n OEt peptides to investigate the network buildup process with time.…”

Section: Results and Discussionmentioning

confidence: 99%

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

et al. 2017

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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.

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Section: Results and Discussionmentioning

confidence: 99%