Abstract
Aiming to build a supersensitive and easily operable immunoassay, bifunctional protein nanowires were generated by seeding-induced self-assembling of the yeast amyloid protein Sup35p that genetically fused with protein G and an enzyme (methyl-parathion hydrolase, MPH), respectively. The protein nanowires possessed a high ratio of enzyme molecules to protein G, allowing a dramatic increase of the enzymatic signal when protein G was bound to an antibody target. As a result, a 100-fold enhancement of the sensitivity was obtained when applied in the detection of the Yersinia pestis F1 antigen.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / analysis
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Enzyme-Linked Immunosorbent Assay*
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Nanowires / chemistry*
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Nerve Tissue Proteins / chemistry
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Nerve Tissue Proteins / genetics
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Peptide Termination Factors / chemistry
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Peptide Termination Factors / genetics
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Phosphoric Monoester Hydrolases / chemistry
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Phosphoric Monoester Hydrolases / genetics
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Saccharomyces cerevisiae Proteins / chemistry
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Saccharomyces cerevisiae Proteins / genetics
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Sensitivity and Specificity
Substances
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Bacterial Proteins
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G-substrate
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Nerve Tissue Proteins
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Peptide Termination Factors
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Recombinant Proteins
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SUP35 protein, S cerevisiae
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Saccharomyces cerevisiae Proteins
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caf1 protein, Yersinia pestis
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Phosphoric Monoester Hydrolases