A novel variable antibody fragment dimerized by the dHLX peptide with enhanced affinity against amantadine compared to its corresponding scFv antibody

Amantadine (AMA) is an illegally used antiviral drug in the poultry industry, it is necessary to establish a fast, accurate and time-saving detection method for poultry food. The antibody-based immunoassay can achieve fast and accurate requirements. We developed a recombinant antibody-based specific...

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Autores principales:	Sanlei Xie, Kai Wen, Tao Peng, Jianyi Wang, Kai Yao, Haiyang Jiang
Formato:	article
Lenguaje:	EN
Publicado:	Taylor & Francis Group 2018
Materias:	amantadine affinity binding ability scfv scfv-dhlx Agriculture (General) S1-972 Immunologic diseases. Allergy RC581-607
Acceso en línea:	https://doaj.org/article/0b2574ae36e6435494a4c957750f213d
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spelling	oai:doaj.org-article:0b2574ae36e6435494a4c957750f213d2021-11-26T11:19:46ZA novel variable antibody fragment dimerized by the dHLX peptide with enhanced affinity against amantadine compared to its corresponding scFv antibody0954-01051465-344310.1080/09540105.2017.1368459https://doaj.org/article/0b2574ae36e6435494a4c957750f213d2018-01-01T00:00:00Zhttp://dx.doi.org/10.1080/09540105.2017.1368459https://doaj.org/toc/0954-0105https://doaj.org/toc/1465-3443Amantadine (AMA) is an illegally used antiviral drug in the poultry industry, it is necessary to establish a fast, accurate and time-saving detection method for poultry food. The antibody-based immunoassay can achieve fast and accurate requirements. We developed a recombinant antibody-based specificity immunoassay for AMA. In the recombinant antibody, the heavy chain variable region (VH) is connected covalently with the light chain variable region (VL) by the artificial linker. Here, two recombinant antibodies’ single-chain variable fragment (scFv) and scFv-dHLX were constructed and functionally expressed in the periplasm of Escherichia coli. The helix-turn-helix peptide was utilized to dimerize VH and VL similar to the IgG counterpart. The ScFv-dHLX protein showed a higher binding ability and affinity resulting in improvement of in vitro affinity activity over its corresponding scFv. Our results not only indicated scFv-dHLX as an alternative for scFv in analytical application, but also offered a novel and efficient hetero-dimerization pattern of VH and VL leading to enhanced affinity.Sanlei XieKai WenTao PengJianyi WangKai YaoHaiyang JiangTaylor & Francis Grouparticleamantadineaffinitybinding abilityscfvscfv-dhlxAgriculture (General)S1-972Immunologic diseases. AllergyRC581-607ENFood and Agricultural Immunology, Vol 29, Iss 1, Pp 244-253 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	amantadine affinity binding ability scfv scfv-dhlx Agriculture (General) S1-972 Immunologic diseases. Allergy RC581-607
spellingShingle	amantadine affinity binding ability scfv scfv-dhlx Agriculture (General) S1-972 Immunologic diseases. Allergy RC581-607 Sanlei Xie Kai Wen Tao Peng Jianyi Wang Kai Yao Haiyang Jiang A novel variable antibody fragment dimerized by the dHLX peptide with enhanced affinity against amantadine compared to its corresponding scFv antibody
description	Amantadine (AMA) is an illegally used antiviral drug in the poultry industry, it is necessary to establish a fast, accurate and time-saving detection method for poultry food. The antibody-based immunoassay can achieve fast and accurate requirements. We developed a recombinant antibody-based specificity immunoassay for AMA. In the recombinant antibody, the heavy chain variable region (VH) is connected covalently with the light chain variable region (VL) by the artificial linker. Here, two recombinant antibodies’ single-chain variable fragment (scFv) and scFv-dHLX were constructed and functionally expressed in the periplasm of Escherichia coli. The helix-turn-helix peptide was utilized to dimerize VH and VL similar to the IgG counterpart. The ScFv-dHLX protein showed a higher binding ability and affinity resulting in improvement of in vitro affinity activity over its corresponding scFv. Our results not only indicated scFv-dHLX as an alternative for scFv in analytical application, but also offered a novel and efficient hetero-dimerization pattern of VH and VL leading to enhanced affinity.
format	article
author	Sanlei Xie Kai Wen Tao Peng Jianyi Wang Kai Yao Haiyang Jiang
author_facet	Sanlei Xie Kai Wen Tao Peng Jianyi Wang Kai Yao Haiyang Jiang
author_sort	Sanlei Xie
title	A novel variable antibody fragment dimerized by the dHLX peptide with enhanced affinity against amantadine compared to its corresponding scFv antibody
title_short	A novel variable antibody fragment dimerized by the dHLX peptide with enhanced affinity against amantadine compared to its corresponding scFv antibody
title_full	A novel variable antibody fragment dimerized by the dHLX peptide with enhanced affinity against amantadine compared to its corresponding scFv antibody
title_fullStr	A novel variable antibody fragment dimerized by the dHLX peptide with enhanced affinity against amantadine compared to its corresponding scFv antibody
title_full_unstemmed	A novel variable antibody fragment dimerized by the dHLX peptide with enhanced affinity against amantadine compared to its corresponding scFv antibody
title_sort	novel variable antibody fragment dimerized by the dhlx peptide with enhanced affinity against amantadine compared to its corresponding scfv antibody
publisher	Taylor & Francis Group
publishDate	2018
url	https://doaj.org/article/0b2574ae36e6435494a4c957750f213d
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A novel variable antibody fragment dimerized by the dHLX peptide with enhanced affinity against amantadine compared to its corresponding scFv antibody

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