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Godzhaev, E. M.; Nuriev, I. R.; Nazarov, A. M.

doi:10.1023/a:1026768823499

Cited by 2 publications

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“…Given the fact that the imidazolyl group of histidine plays an important role in the catalytic process of native hydrolase (e.g. : chymotrypsin, 37 trypsin, 38 acetylcholine esterase, 39 and kidney dialkyluorophosphatase 40 ), herein we designed and synthesized an imidazolyl-containing amphiphilic tripeptide N-(uorenyl-9-methoxycarbonyl)-Phe-Phe-His-NH 2 (Fmoc-FFH-CONH 2 ) hoping to exploit it to construct a novel supramolecular peptide hydrolase model with high catalytic activity, good biocompatibility and based on it to study the relationships between the ordered arrangement of the supramolecular structures and the catalytic activity. We use peptides as scaffolds because the exible structures of peptides do make it possible to put the special functional residues of complex proteins into simple molecules, which could further selfassemble into supramolecular structures with abundant orderly arranged functional groups that have many unexpected properties.…”

Section: Introductionmentioning

confidence: 99%

Self-assembly of amphiphilic peptides into bio-functionalized nanotubes: a novel hydrolase model

et al. 2013

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Herein, we report the construction of a novel hydrolase model via self-assembly of a synthetic amphiphilic short peptide (Fmoc-FFH-CONH 2 ) into nanotubes. The peptide-based self-assembled nanotubes (PepNTs-His) with imidazolyl groups as the catalytic centers exhibit high catalytic activity for p-nitrophenyl acetate (PNPA) hydrolysis. By replacement of the histidine of Fmoc-FFH-CONH 2 with arginine to produce a structurally similar peptide Fmoc-FFR-CONH 2 , guanidyl groups can be presented in the nanotubes through the co-assembly of these two molecules to stabilize the transition state of the hydrolytic reaction. Therefore significantly improved catalytic activity has been achieved by the reasonable distribution of three dominating catalytic factors: catalytic center, binding site and transition state stabilization to the co-assembled peptide nanotubes (PepNTs-His-Arg max ). The resulting hydrolase model shows typical saturation kinetics behaviour to that of natural enzymes and the catalytic efficiency of a single catalytic center is 519-fold higher than that without catalysts. As for a nanotube with multicatalytic centers, a remarkable catalytic efficiency could be achieved with the increase of building blocks. This model suggests that the well ordered and dynamic supramolecular structure is an attractive platform to develop new artificial enzymes to enhance the catalytic activity. Besides, this novel peptidebased material has excellent biocompatibility with human cells and is expected to be applied to organisms as a substitute for natural hydrolases.

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Section: Introductionmentioning

confidence: 99%

Self-assembly of amphiphilic peptides into bio-functionalized nanotubes: a novel hydrolase model

et al. 2013

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“…Most of the synthetic particles investigated have spherical symmetry and lack the internal order which is characteristic of proteins. The use of imidazolyl groups in artificial catalysts has been popular given the presence of histidine residues at the catalytic site of several hydrolytic enzymes including acetylcholine esterase, chymotrypsin, trypsin, and kidney dialkylfluorophosphatase . A considerable increase of reaction rates has been observed upon aggregation of active sites, presumably due to the increase in concentration of reaction loci and cooperativity among functional groups …”

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A Self-Assembled Nanofiber Catalyst for Ester Hydrolysis

2007

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Catalytic particles based on supramolecular systems have demonstrated significant improvement in the field of catalysis. In this work, histidine-functionalized self-assembling peptide amphiphiles (PAs) were synthesized in order to form self-assembly high-aspect-ratio nanofibers with internal order that can present imidazolyl groups capable of ester hydrolysis. Self-assembly of the molecules making up the catalytic particle was studied by transmission electron microscopy and circular dichroism. The reactive sites were designed with histidine residues to catalyze the hydrolysis of 2,4-dinitrophenyl acetate (DNPA). Enzymatic hydrolysis of DNPA was observed in the presence of the nanofibers by UV−vis spectroscopy and the Michaelis−Menten enzyme kinetics model. Significantly faster hydrolysis rate was observed in the presence of self-assembled nanofibers relative to spherical aggregates expected to have less order as well as single molecule catalysts.

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Cited by 2 publications

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Self-assembly of amphiphilic peptides into bio-functionalized nanotubes: a novel hydrolase model

Self-assembly of amphiphilic peptides into bio-functionalized nanotubes: a novel hydrolase model

A Self-Assembled Nanofiber Catalyst for Ester Hydrolysis

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