Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.biopha.2021.111328
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dc.titleDesigning and constructing a phage display synthesized single domain antibodies library based on camel VHHs frame for screening and identifying humanized TNF-?-specific nanobody
dc.contributor.authorNie, Jifan
dc.contributor.authorMa, Xingyuan
dc.contributor.authorHu, Fabiao
dc.contributor.authorMiao, Hui
dc.contributor.authorFeng, Xin
dc.contributor.authorZhang, Peiwen
dc.contributor.authorHan, Myong Hun
dc.contributor.authorYou, Fang
dc.contributor.authorYang, Yi
dc.contributor.authorZhang, Wenlian
dc.contributor.authorZheng, Wenyun
dc.date.accessioned2022-10-13T07:52:03Z
dc.date.available2022-10-13T07:52:03Z
dc.date.issued2021-05-01
dc.identifier.citationNie, Jifan, Ma, Xingyuan, Hu, Fabiao, Miao, Hui, Feng, Xin, Zhang, Peiwen, Han, Myong Hun, You, Fang, Yang, Yi, Zhang, Wenlian, Zheng, Wenyun (2021-05-01). Designing and constructing a phage display synthesized single domain antibodies library based on camel VHHs frame for screening and identifying humanized TNF-?-specific nanobody. Biomedicine and Pharmacotherapy 137 : 111328. ScholarBank@NUS Repository. https://doi.org/10.1016/j.biopha.2021.111328
dc.identifier.issn0753-3322
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/233206
dc.description.abstractTumor necrosis factor (TNF-?) is an important clinically tested cytokine that could induce autoimmune diseases and inflammation. Therefore, the anti-TNF-? therapy strategy was developed and used therapeutically in various diseases, especially in the cytokine storm associated chimeric antigen receptor (CAR) T-cell therapy and antiviral therapy. Compare with other anti-TNF-? inhibitors, anti-TNF-? Nb (nanobody) has many unique advantages. Herein, we reported a novel humanized scaffold for library construction, which could be soluble and expressed in Escherichia coli (E.coli), and the efficiency capacity could reach as high as 2.01 × 109. Meanwhile, an anti-TNF-? Nb was selected for further study after 4 rounds of screening, NT-3, as the optimal Nb could effectively inhibit TNF-mediated cytotoxicity. The IC50 of NT-3 was determined as 0.804 ?M, and its apoptosis inhibition rate was 62.47 % in L929 cells. Furthermore, the molecular docking results showed that complementarity-determining regions (CDRs) of NT-3 could connect to TNF for blocking function through strong hydrogen bonds and salt bridges. In general, our study not only provided a good Nb screening platform in vitro without animal immunization, but also generated a series of novel humanized anti-TNF-? Nb candidates with potential applications. © 2021
dc.publisherElsevier Masson s.r.l.
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 International
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/
dc.sourceScopus OA2021
dc.subjectDesigning and constructing
dc.subjectHumanized TNF-?-specific Nb
dc.subjectPhage display library
dc.subjectScreening and identifyin
dc.subjectSingle domain antibodies
dc.typeArticle
dc.contributor.departmentNUS ENVIRONMENTAL RESEARCH INSTITUTE
dc.description.doi10.1016/j.biopha.2021.111328
dc.description.sourcetitleBiomedicine and Pharmacotherapy
dc.description.volume137
dc.description.page111328
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