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• W2158502922 abstract "Most immunoassays for determination of small molecules are still designed on the basis of the “trial and error” method, due to the lack of understanding of antibody recognition. In the present study, we developed a heterologous indirect competitive enzyme-linked immunosorbent assay for determination of triazine herbicides, with limits of detection for 11 triazines ranging from 0.05 to 29.4 μg/L. Mechanisms of the antigen–antibody interaction were studied by computer-aided molecular modeling (CAMM)-based quantitative structure–activity relationship analyses. Co-effects of the analytes’ substructural hydrophobic, electrostatic, and steric fields on antibody recognition were further revealed. Hydrophobicity of the antigens was demonstrated to have the most important impact. Even less exposed substituents provided hydrophobic force to the antigen–antibody interaction. Dislocated orientation of analyte functional groups could lead to steric hindrance and hydrophobic misleading of antibody recognition. This may happen even when the antigens contained the same substituent as the hapten. Frontier orbital energies also affect the reaction significantly. This study highlights of the power of CAMM-based analyses, providing insights into antibody recognition of small molecules." @default.
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• W2158502922 date "2012-10-16" @default.
• W2158502922 modified "2023-10-14" @default.
• W2158502922 title "Computer-Aided Molecular Modeling Study on Antibody Recognition of Small Molecules: An Immunoassay for Triazine Herbicides" @default.
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• W2158502922 doi "https://doi.org/10.1021/jf303256r" @default.
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