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Development of an efficient signal amplification strategy for label-free enzyme immunoassay using two site-specific biotinylated recombinant proteins.
Tang, Jin-Bao; Tang, Ying; Yang, Hong-Ming.
Afiliación
  • Tang JB; School of Pharmacy, Weifang Medical University, Weifang 261053, PR China.
  • Tang Y; Affiliated Hospital of Weifang Medical University, Weifang 261041, PR China.
  • Yang HM; School of Pharmacy, Weifang Medical University, Weifang 261053, PR China. Electronic address: yanghongming2006@sohu.com.
Anal Chim Acta ; 859: 66-71, 2015 Feb 15.
Article en En | MEDLINE | ID: mdl-25622607
Constructing a recombinant protein between a reporter enzyme and a detector protein to produce a homogeneous immunological reagent is advantageous over random chemical conjugation. However, the approach hardly recombines multiple enzymes in a difunctional fusion protein, which results in insufficient amplification of the enzymatic signal, thereby limiting its application in further enhancement of analytical signal. In this study, two site-specific biotinylated recombinant proteins, namely, divalent biotinylated alkaline phosphatase (AP) and monovalent biotinylated ZZ domain, were produced by employing the Avitag-BirA system. Through the high streptavidin (SA)-biotin interaction, the divalent biotinylated APs were clustered in the SA-biotin complex and then incorporated with the biotinylated ZZ. This incorporation results in the formation of a functional macromolecule that involves numerous APs, thereby enhancing the enzymatic signal, and in the production of several ZZ molecules for the interaction with immunoglobulin G (IgG) antibody. The advantage of this signal amplification strategy is demonstrated through ELISA, in which the analytical signal was substantially enhanced, with a 32-fold increase in the detection sensitivity compared with the ZZ-AP fusion protein approach. The proposed immunoassay without chemical modification can be an alternative strategy to enhance the analytical signals in various applications involving immunosensors and diagnostic chips, given that the label-free IgG antibody is suitable for the ZZ protein.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Inmunoglobulinas / Técnicas para Inmunoenzimas / Fosfatasa Alcalina Límite: Animals Idioma: En Revista: Anal Chim Acta Año: 2015 Tipo del documento: Article Pais de publicación: Países Bajos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Inmunoglobulinas / Técnicas para Inmunoenzimas / Fosfatasa Alcalina Límite: Animals Idioma: En Revista: Anal Chim Acta Año: 2015 Tipo del documento: Article Pais de publicación: Países Bajos