2012
DOI: 10.1039/c2cc32863a
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Immobilization of engineered arginase on gold-carbon nanotubes

Abstract: It is demonstrated that engineered arginase with a single protruded site of cysteine deliberately placed away from its active centre by site-directed mutagenesis can facilitate its attachment on a gold-nanoparticle surface with atomic precision, resulting in no apparent loss in enzymatic activity.

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Cited by 7 publications
(3 citation statements)
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“…Although the metal binding and other residues are conserved (Figure ) in H. pylori arginase, we sought to investigate the role of the unique stretch of sequence motif which could provide structural and functional insight into this enzyme. Moreover, the increased interests for the search of arginase-based therapeutics and design of effective anticarcinogenic arginase from prokaryotes to eukaryotes have drawn considerable attention . Various forms of human arginase I such as pegylated, Co 2+ -reconstituted and the chimeric protein of human arginase I and human arginase II have been attempted to test the anticancer efficacy. In the present report, we have undertaken a combination of approaches that include deletion of the sequence, kinetic assays, site-directed mutagenesis, metal analysis, circular dichroism, analytical gel-filtration assay, heat-induced denaturation and molecular dynamics (MD) simulations to investigate the location of the sequence motif and whether the entire sequence or its individual residue has impact on the kinetics, bimetallic site, structure, and stability of the protein.…”
mentioning
confidence: 99%
“…Although the metal binding and other residues are conserved (Figure ) in H. pylori arginase, we sought to investigate the role of the unique stretch of sequence motif which could provide structural and functional insight into this enzyme. Moreover, the increased interests for the search of arginase-based therapeutics and design of effective anticarcinogenic arginase from prokaryotes to eukaryotes have drawn considerable attention . Various forms of human arginase I such as pegylated, Co 2+ -reconstituted and the chimeric protein of human arginase I and human arginase II have been attempted to test the anticancer efficacy. In the present report, we have undertaken a combination of approaches that include deletion of the sequence, kinetic assays, site-directed mutagenesis, metal analysis, circular dichroism, analytical gel-filtration assay, heat-induced denaturation and molecular dynamics (MD) simulations to investigate the location of the sequence motif and whether the entire sequence or its individual residue has impact on the kinetics, bimetallic site, structure, and stability of the protein.…”
mentioning
confidence: 99%
“…In recent years, one-dimensional SWNTs, containing p-conjugated aromatic carbon atoms, have attracted tremendous attention as promising materials for fundamentals tudies and applications.A mongm any unique properties,S WNTse xhibit excellent electric conductivity,w hich renders them ideal candidates for materials in electronic devices. [5] Recently,c omposites consisting of SWNTsa nd various functional materials such as organic molecules, [6] polymers, [7] metallic/semiconducting nano-particles, [8] or proteins [9] have been fabricated. Due to the large surfacea rea and excellentc onductivity of SWNTsi nc ombination with the possibility to introduce new electronic and photonic properties through the functional materials, practical applications fors uch composites can be easily envisioned in the context of electronics and sensors.…”
Section: Mðiiþ-bl-mðiiþmentioning
confidence: 99%
“…In fact, in most MNP immobilization processes, the enzymes are immobilized via cross-linking to improve their performances . Covalent bonds are usually more efficient in recycling, and sometimes, they can achieve oriented immobilization. , As we know, most oriented immobilization is needed to coat carriers with organic reagents or other materials with functional groups; , for example, the formation of reversible Au–S bonds for trypsin immobilization, which preserved the native conformation of the trypsin well, but this method is not applicable to MNPs. In addition, coimmobilization was another effective way to maximize the recovery rate of activity and maintain the structure of the enzymes .…”
Section: Introductionmentioning
confidence: 99%