A Simple Protocol for the Modular Assembly of “Millipede” Artificial Enzymes

Motherwell, William B.; Atkinson, Catherine E.; Aliev, Abil E.; Wong, Stephanie Y. F.; Warrington, Brian H.

doi:10.1002/anie.200352370

Cited by 11 publications

(6 citation statements)

References 30 publications

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“…In the past several decades, considerable efforts have been made to employ various strategies to mimic natural enzymes, such as organic synthesis, [1][2][3][4] semi-synthesis, 5 molecular imprinting, 6,7 genetic engineering and so on. 8,9 Although the strategies mentioned above are effective to simulate enzymes with extremely high activity and other excellent properties, they are unable to achieve the reasonable match among the catalytic factors of enzymes due to the lack of dynamic ordered structures caused by their stable covalent interactions.…”

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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“…As previously reported, [42,48] the use of a succinimidyl ester of the desired carboxylic acid was quite successful for tethering to amine groups. We initially focussed on using 2-acetoxybenzoic acid (more commonly known as Aspirin) as our pendant group.…”

Section: Resultsmentioning

confidence: 55%

“…Due to the diversity of the groups we desired to attach to the PAH-H backbone, we knew that using any aqueous media as a solvent would affect the yield. Tanaka et al [47] and subsequently Atkinson et al [42,48] had reported the conversion of PAH into PAH-H via simple addition of a Brønsted-Lowry base (KOH in methanol) followed by precipitation to remove the salt by-product. We attempted using this route with several other bases including diisopropylethylamine and NaH, however, we were unsuccessful.…”

Section: Resultsmentioning

confidence: 99%

Thermal and Spectral Analysis of Novel Amide-Tethered Polymers from Poly(allylamine)

et al. 2016

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Post-polymerization modification of poly(allylamine hydrochloride) was applied to synthesize a library of amide-linked polyelectrolytes with tethered aliphatic, aromatic, and cubyl moieties. The efficacy of amidation was determined to be between 12 and 98 %, depending on the electronics, sterics, and solubility of the amide linkage. 13 C solid-state NMR was used to further validate their structure. Thermogravimetric analysis and differential scanning calorimetry analysis indicated that none of the new polymers displayed a classic melt/freeze profile, but all displayed onset decomposition temperatures smaller than 2158C. We anticipate that the structure-property relationships observed in the resulting library of graft-modified polymers can facilitate better understanding of how to design polyelectrolytes for the construction of well-defined multilayer systems.

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“…The design and synthesis of artificial catalysts with natural enzymatic performance is one of the goals that has always been pursued by a great many scientists. The past couple of decades have witnessed a rapid evolution in the development of novel artificial enzymes employing various strategies, such as organic synthesis, molecular imprinting, supramolecular chemistry, semi‐synthesis, genetic engineering and so on 2–30. The primary attempts in the design of artificial enzymes have mainly focused on the construction of macrocyclic compounds carrying catalytic moieties for substrate recognition and catalysis.…”

Section: Introductionmentioning

confidence: 99%

“…Thus, typical scaffolds include cyclodextrins, cyclophanes, calixarene mimics and other macrocyclic compounds 2, 6–10, 22, 24, 25. Apart from synthesized macrocyclic compounds, macromolecule‐based scaffolds, such as synthesized dendrimer, hydrogels21 and polymers,22, 23 as well as biomacromolecules11, 12 with specific recognition for substrates,11–18 and more importantly, for transition states have been developed 15. Recently, the design concept of nanozyme may open up a new way to design more complicated enzyme models 19, 20.…”

Section: Introductionmentioning

confidence: 99%

Design of Artificial Selenoenzymes Based on Macromolecular Scaffolds

Huang

Yin

2010

Macromolecular Bioscience

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The selenoenzyme glutathione peroxidase has received increased attention as one of the antioxidative enzymes exerting important biological roles in living bodies. Over the past decades, much effort has been invested to mimic its catalytic behavior for understanding enzymatic catalytic mechanisms and also for developing potential medicines. A great number of artificial GPxs, ranging from small molecular compounds to macromolecular ones, have been designed and prepared by combining the concept of recognition and catalysis using chemical, biological and supramolecular strategies. In this article, we specify the development of artificial GPxs based on macromolecules as scaffolds, and discuss the power of reduced models in studying the bio-catalytic nature of selenoenzymes.

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A Simple Protocol for the Modular Assembly of “Millipede” Artificial Enzymes

Cited by 11 publications

References 30 publications

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

Thermal and Spectral Analysis of Novel Amide-Tethered Polymers from Poly(allylamine)

Design of Artificial Selenoenzymes Based on Macromolecular Scaffolds

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