Size-dependent tuning of horseradish peroxidase bioreactivity by gold nanoparticlesElectronic supplementary information (ESI) available. See DOI: 10.1039/c4nr07056a
Molecules with diverse biological functions, such as heme peroxidases, can be useful tools for identifying potential biological effects of gold nanoparticles (AuNPs) at the molecular level. Here, using UV-Vis, circular dichroism, dynamic light scattering, and electron spin resonance spectroscopy, we...
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Main Authors | , , , , , , |
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Format | Journal Article |
Language | English |
Published |
26.02.2015
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Online Access | Get full text |
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Summary: | Molecules with diverse biological functions, such as heme peroxidases, can be useful tools for identifying potential biological effects of gold nanoparticles (AuNPs) at the molecular level. Here, using UV-Vis, circular dichroism, dynamic light scattering, and electron spin resonance spectroscopy, we report tuning of horseradish peroxidase (HRP) bioactivity by reactant-free AuNPs with diameters of 5, 10, 15, 30 and 60 nm (Au-5 nm, Au-10 nm, Au-15 nm, Au-30 nm and Au-60 nm). HRP conjugation to AuNPs was observed with only Au-5 nm and Au-10 nm prominently increasing the α-helicity of the enzyme to extents inversely related to their size. Au-5 nm inhibited both HRP peroxidase activity toward 3,3′,5,5′-tetramethylbenzidine and HRP compound I/II reactivity toward 5,5-dimethyl-1-pyrroline
N
-oxide. Au-5 nm enhanced the HRP peroxidase activity toward ascorbic acid and the HRP compound I/II reactivity toward redox-active residues in the HRP protein moiety. Further, Au-5 nm also decreased the catalase- and oxidase-like activities of HRP. Au-10 nm showed similar, but weaker effects, while Au-15 nm, Au-30 nm and Au-60 nm had no effect. Results suggest that AuNPs can size-dependently enhance or inhibit HRP bioreactivity toward substrates with different redox potentials
via
a mechanism involving extension of the HRP substrate access channel and decline in the redox potentials of HRP catalytic intermediates.
Here we report gold nanoparticles can size-dependently enhance or inhibit HRP bioreactivity toward substrates with different redox potentials
via
a mechanism involving extension of the HRP substrate access channel and decline in the redox potentials of HRP catalytic intermediates. |
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Bibliography: | 10.1039/c4nr07056a Electronic supplementary information (ESI) available. See DOI |
ISSN: | 2040-3364 2040-3372 |
DOI: | 10.1039/c4nr07056a |