Journal
ACS APPLIED MATERIALS & INTERFACES
Volume 10, Issue 30, Pages 25113-25120Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acsami.8b07225
Keywords
ELISA; MOF composite; colorimetric immunoassay; IgG; peroxidase mimic
Funding
- Natural Science Foundation of China [21765010, 21305054]
- Natural Science Foundation of Jiangxi Province [20151BAB203020]
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Enzyme-linked immunosorbent assay has been widely used as a gold standard in biomedical field, but some inevitable drawbacks still exist in its practical applications, especially the laborious preparation of enzyme-antibody conjugates by a covalent linkage. In this work, we proposed a new strategy to prepare enzyme-antibody conjugate by integrating antibody with catalytic metal-organic framework (MOF) to form dual-functional MOF/antibody composite. As models, rabbit antimouse immunoglobulin G antibody (RIgG) and Cu-MOF with peroxidase-like activity were used to fabricate RIgG@Cu-MOF composite for colorimetric immunoassay. It was found that Cu-MOF as a host not only has no influence on the original capture ability of RIgG to its corresponding antigen (mIgG), but also can shield RIgG against long-term storage, high temperature, and biological degradation. More importantly, upon the formation of sandwiched immunocomplex between RIgG@Cu-MOF and capture antibody, Cu-MOF can serve as a signal amplification unit to perform colorimetric immunoassay. The detection limit of RIgG@Cu-MOF toward mIgG was obtained at 0.34 ng/mL, which is 3-fold lower than that of horseradish peroxidase labeled RIgG. Furthermore, the successful determination of mIgG in serum sample demonstrates the applicability of RIgG@Cu-MOF in detecting real sample. Therefore, it is highly anticipated that this study can offer a new way to prepare enzyme-antibody conjugates, facilitating the exploration of MOF composites in biomedical field.
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