Journal
ANALYTICAL CHEMISTRY
Volume 94, Issue 4, Pages 2109-2118Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.analchem.1c04448
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Funding
- National Natural Science Foundation of China [61875114]
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A sensitive surface plasmon resonance (SPR) assay was developed for LECT2 analysis, with a detection limit of 10.93 pg/mL. The immobilization method improved the binding efficiency of Tie1 protein, and this strategy could be extended to attach antibodies or recombinant Fc label proteins.
Leukocyte cell-derived chemotaxin 2 (LECT2) has been proved to be a potential biomarker for the diagnosis of liver fibrosis. In this work, a sensitive surface plasmon resonance (SPR) assay for LECT2 analysis was developed. Tyrosine kinase with immune globulin-like and epidermal growth factor-like domains 1 (Tie1) is an orphan receptor of LECT2 with a C-terminal Fc tag, which is far away from the LECT2 binding sites. The Fc aptamer was intentionally used to capture the Tie1 through its Fc tag, connecting with Fe3O4-coated silver magnetic nanoparticles (Ag@MNPs) and ensuring the LECT2 binding site to be outward. Attributed to the orientation nature of the captured protein, Ag@MNPs were able to enhance the SPR signal. A sensitive LECT2 sensor was successfully fabricated with a detection limit of 10.93 pg/mL. The results showed that the immobilization method improved the binding efficiency of Tie1 protein. This strategy could be extended to attach antibodies or recombinant Fc label proteins to Fc aptamer-based nanoparticles.
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