ArticleAnalytical and bioanalytical chemistry2026
Structural basis of a CDR3-embedded binding mechanism in a nanobody for sensitivity enhancement toward tenuazonic acid.
Article in Analytical and bioanalytical chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Nanobodies (Nbs) have shown great potential for use in immunoassays targeting small-molecule contaminants in food safety monitoring. However, a limited understanding of their recognition mechanisms has hindered the development of high-performance Nbs and the improvement of assay performance. Herein, a previously developed nanobody (Nb) 3F9 against tenuazonic acid (TeA) was selected as a model to resolve its X-ray crystal structure. Notably, Nb3F9 adopts a typical immunoglobulin fold, with TeA deeply inserted into the complementary-determining region 3 (CDR3) and buried in a binding pocket formed by Phe37, Ser99, Tyr107, Arg110, Asp112, Met113, Asp114, Pro115, Arg117, and Gly118. Based on this insight, integrating computational prediction with site-directed mutagenesis, a mutant Nb3F9-Y107K was obtained, achieving an 8.6-fold increase in sensitivity while maintaining excellent stability and high specificity compared with the wild-type. It is believed that this work provides a rational framework for improving the binding activity of Nbs and expanding their applications in food safety.
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