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A novel bivalent single‐chain variable fragment (scFV) inhibits the action of tumour necrosis factor α
Author(s) -
Liu Mengyuan,
Wang Xiangbin,
Yin Changcheng,
Zhang Zhong,
Lin Qing,
Zhen Yongsu,
Huang Hualiang
Publication year - 2008
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1042/ba20070229
Subject(s) - tumor necrosis factor alpha , avidity , bivalent (engine) , peptide , chemistry , single chain variable fragment , escherichia coli , necrosis , microbiology and biotechnology , antibody , biology , biochemistry , recombinant dna , immunology , gene , genetics , organic chemistry , metal
Suppression of TNFα (tumour necrosis factor α) activity is widely considered to be among the most efficient treatments available for chronic inflammatory diseases. Here, a bivalent scFv (single‐chain variable fragment) fragment, named TNF‐BAb, was engineered by fusing two anti‐TNFα scFV fragments in tandem via a long and flexible linking peptide derived from human serum albumin and produced in functional form from Escherichia coli inclusion bodies. The bioactivity assays demonstrated that TNF‐BAb gained enormously in avidity and showed a much stronger ability to inhibit the biological action of TNFα, indicating that TNF‐BAb may become a good candidate for anti‐TNFα therapy.