Data

Data from: Competitive Inhibition of the Enzyme-Mimic Activity of Gd-Based Nanorods toward Highly Specific Colorimetric Sensing of l‑Cysteine

RMIT University, Australia
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ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Adc&rfr_id=info%3Asid%2FANDS&rft_id=https://figshare.com/articles/Competitive_Inhibition_of_the_Enzyme-Mimic_Activity_of_Gd-Based_Nanorods_toward_Highly_Specific_Colorimetric_Sensing_of_l_Cysteine/5378221&rft.title=Data from: Competitive Inhibition of the Enzyme-Mimic Activity of Gd-Based Nanorods toward Highly Specific Colorimetric Sensing of l‑Cysteine&rft.identifier=6c7c88aae6c1e23cf6d1d3505ecc3431&rft.publisher=RMIT University, Australia&rft.description=Attached file provides supplementary data for linked article. Gd-based nanomaterials offer interesting magnetic properties and have been heavily investigated for magnetic resonance imaging. The applicability of these materials beyond biomedical imaging remains limited. The current study explores the applicability of these rare-earth nanomaterials as nanozyme-mediated catalysts for colorimetric sensing of l-cysteine, an amino acid of high biomedical relevance. We show a facile solution-based strategy to synthesize two Gd-based nanomaterials viz. Gd(OH)3 and Gd2O3 nanorods. We further establish the catalytic peroxidase-mimic nanozyme activity of these Gd(OH)3 and Gd2O3 nanorods. This catalytic activity was suppressed specifically in the presence of l-cysteine that allowed us to develop a colorimetric sensor to detect this biologically relevant molecule among various other contaminants. This suppression, which could either be caused due to catalyst poisoning or enzyme inhibition, prompted extensive investigation of the kinetics of this catalytic inhibition in the presence of cysteine. This revealed a competitive inhibition process, a mechanism akin to those observed in natural enzymes, bringing nanozymes a step closer to the biological systems.&rft.creator=Anonymous&rft.date=2018&rft.relation=http://pubs.acs.org/doi/abs/10.1021/acs.langmuir.7b01926&rft_rights=Further information about rights and usage of ACS publications and supplementary data can be found here: http://pubs.acs.org/page/copyright/permissions.html.&rft_rights=CC BY-NC: Attribution-Noncommercial 3.0 AU http://creativecommons.org/licenses/by-nc/3.0/au&rft_subject=Enzyme&rft_subject=Nanomaterials&rft_subject=Magnetic resonance imaging&rft_subject=Catalytic peroxidase-mimic nanozyme activity&rft_subject=Competitive inhibition process&rft_subject=Nanomaterials&rft_subject=TECHNOLOGY&rft_subject=NANOTECHNOLOGY&rft.type=dataset&rft.language=English Access the data

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CC BY-NC: Attribution-Noncommercial 3.0 AU
http://creativecommons.org/licenses/by-nc/3.0/au

Further information about rights and usage of ACS publications and supplementary data can be found here: http://pubs.acs.org/page/copyright/permissions.html.

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Attached file provides supplementary data for linked article. Gd-based nanomaterials offer interesting magnetic properties and have been heavily investigated for magnetic resonance imaging. The applicability of these materials beyond biomedical imaging remains limited. The current study explores the applicability of these rare-earth nanomaterials as nanozyme-mediated catalysts for colorimetric sensing of l-cysteine, an amino acid of high biomedical relevance. We show a facile solution-based strategy to synthesize two Gd-based nanomaterials viz. Gd(OH)3 and Gd2O3 nanorods. We further establish the catalytic peroxidase-mimic nanozyme activity of these Gd(OH)3 and Gd2O3 nanorods. This catalytic activity was suppressed specifically in the presence of l-cysteine that allowed us to develop a colorimetric sensor to detect this biologically relevant molecule among various other contaminants. This suppression, which could either be caused due to catalyst poisoning or enzyme inhibition, prompted extensive investigation of the kinetics of this catalytic inhibition in the presence of cysteine. This revealed a competitive inhibition process, a mechanism akin to those observed in natural enzymes, bringing nanozymes a step closer to the biological systems.

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  • Local : 6c7c88aae6c1e23cf6d1d3505ecc3431
ACN 633 798 857