Phage anti-immune complex assay: General strategy for noncompetitive immunodetection of small molecules

A. González-Techera, L. Vanrell, Jerold A Last, B. D. Hammock, G. González-Sapienza

Research output: Contribution to journalArticle

39 Scopus citations

Abstract

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 bearing 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

Original languageEnglish (US)
Pages (from-to)7799-7806
Number of pages8
JournalAnalytical Chemistry
Volume79
Issue number20
DOIs
StatePublished - Oct 15 2007

ASJC Scopus subject areas

  • Analytical Chemistry

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