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Highly sensitive and robust peroxidase-like activity of Au-Pt core/shell nanorod-antigen conjugates for measles virus diagnosis.


ABSTRACT: BACKGROUND:As a promising candidate for artificial enzymes, catalytically active nanomaterials show several advantages over natural enzymes, such as controlled synthesis at low cost, tunability of catalytic activities, and high stability under stringent conditions. Rod-shaped Au-Pt core/shell nanoparticles (Au@Pt NRs), prepared by Au nanorod-mediated growth, exhibit peroxidase-like activities and could serve as an inexpensive replacement for horseradish peroxidase, with potential applications in various bio-detections. The determination of measles virus is accomplished by a capture-enzyme-linked immunosorbent assay (ELISA) using Au@Pt NR-antigen conjugates. RESULTS:Based on the enhanced catalytic properties of this nanozyme probe, a linear response was observed up to 10 ng/mL measles IgM antibodies in human serum, which is 1000 times more sensitive than commercial ELISA. CONCLUSIONS:Hence, these findings provide positive proof of concept for the potential of Au@Pt NR-antigen conjugates in the development of colorimetric biosensors that are simple, robust, and cost-effective.

SUBMITTER: Long L 

PROVIDER: S-EPMC5930499 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature

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Highly sensitive and robust peroxidase-like activity of Au-Pt core/shell nanorod-antigen conjugates for measles virus diagnosis.

Long Lin L   Liu Jianbo J   Lu Kaishun K   Zhang Tao T   Xie Yunqing Y   Ji Yinglu Y   Wu Xiaochun X  

Journal of nanobiotechnology 20180502 1


<h4>Background</h4>As a promising candidate for artificial enzymes, catalytically active nanomaterials show several advantages over natural enzymes, such as controlled synthesis at low cost, tunability of catalytic activities, and high stability under stringent conditions. Rod-shaped Au-Pt core/shell nanoparticles (Au@Pt NRs), prepared by Au nanorod-mediated growth, exhibit peroxidase-like activities and could serve as an inexpensive replacement for horseradish peroxidase, with potential applica  ...[more]

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