Oriented immobilization of antibodies through peptide ligands for ultrasensitive detection of gastrin 17 in human serum via lateral flow immunoassay

Li, Xintong; Cui, Jiale; Li, Jin; Wang, Yulian; Shi, Guoqing

doi:10.1016/j.microc.2024.110819

Microchemical Journal

2024

DOI: 10.1016/j.microc.2024.110819

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Oriented immobilization of antibodies through peptide ligands for ultrasensitive detection of gastrin 17 in human serum via lateral flow immunoassay

Xintong Li,

Jiale Cui,

Jin Li

et al.

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2024

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Cited by 1 publication

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Fabrication of a Heptapeptide-Modified Poly(glycidyl Methac-Rylate) Nanosphere for Oriented Antibody Immobilization and Immunoassay

Gong,

Zhang,

Zhu

et al. 2024

Molecules

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Oriented antibody immobilization has been widely employed in immunoassays and immunodiagnoses due to its efficacy in identifying target antigens. Herein, a heptapeptide ligand, HWRGWVC (HC7), was coupled to poly(glycidyl methacrylate) (PGMA) nanospheres (PGMA-HC7). The antibody immobilization behavior and antigen recognition performance were investigated and compared with those on PGMA nanospheres by nonspecific adsorption and covalent coupling via carbodiimide chemistry. The antibodies tested included bovine, rabbit, and human immunoglobulin G (IgG), while the antigens included horseradish peroxidase (HRP) and β-2-Microglobulin (β2-MG). The nanospheres were characterized using zeta potential and particle size analyzers, scanning electron microscopy, transmission electron microscopy, Fourier transform infrared spectroscopy, and reversed-phase chromatography, proving each synthesis step was succeeded. Isothermal titration calorimetry assay demonstrated the strong affinity interaction between IgG and PGMA-HC7. Notably, PGMA-HC7 achieved rapid and extremely high IgG adsorption capacity (~3 mg/mg) within 5 min via a specific recognition via HC7 without nonspecific interactions. Moreover, the activities of immobilized anti-HRP and anti-β2-MG antibodies obtained via affinity binding were 1.5-fold and 2-fold higher than those of their covalent coupling counterparts. Further, the oriented-immobilized anti-β2-MG antibody on PGMA-HC7 exhibited excellent performance in antigen recognition with a linear detection range of 0–5.3 μg/mL, proving its great potential in immunoassay applications.

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Fabrication of a Heptapeptide-Modified Poly(glycidyl Methac-Rylate) Nanosphere for Oriented Antibody Immobilization and Immunoassay

Gong,

Zhang,

Zhu

et al. 2024

Molecules

View full text Add to dashboard Cite

show abstract

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Oriented immobilization of antibodies through peptide ligands for ultrasensitive detection of gastrin 17 in human serum via lateral flow immunoassay

Cited by 1 publication

References 36 publications

Fabrication of a Heptapeptide-Modified Poly(glycidyl Methac-Rylate) Nanosphere for Oriented Antibody Immobilization and Immunoassay

Fabrication of a Heptapeptide-Modified Poly(glycidyl Methac-Rylate) Nanosphere for Oriented Antibody Immobilization and Immunoassay

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