Journal
ANALYTICAL CHEMISTRY
Volume 79, Issue 20, Pages 7799-7806Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ac071323h
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Funding
- FIC NIH HHS [TW05718, D43 TW005718, D43 TW005718-06] Funding Source: Medline
- NIEHS NIH HHS [P30 ES005707, P30 ES05707, P42 ES004699-170005, P42 ES004699, P42 ES04699] Funding Source: Medline
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Due to their size, small molecules cannot be simultaneously bound by two antibodies, precluding their detection by noncompetitive two-site immunoassays, which are superior to competitive ones in terms of sensitivity, kinetics, and working range. This has prompted the development of anti-immune complex antibodies, but these are difficult to produce, and often exhibit high cross-reactivity with the unliganded primary antibody. This work demonstrates that anti-immune complex antibodies can be substituted by phage particles isolated from phage display peptide libraries. Phages beating specific small peptide loops allowed to focus the recognition to changes in the binding area of the immune complex. The concept was tested using environmental and drug analytes; with improved sensitivity and ready adaptation into on-site formats. Peptides specific for different immune complexes can be isolated from different peptide libraries in a simple and systematic fashion allowing the rapid development of noncompetitive assays for small molecules.
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