Please use this identifier to cite or link to this item:
https://doi.org/10.1016/j.biopha.2021.111328
DC Field | Value | |
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dc.title | Designing 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.author | Nie, Jifan | |
dc.contributor.author | Ma, Xingyuan | |
dc.contributor.author | Hu, Fabiao | |
dc.contributor.author | Miao, Hui | |
dc.contributor.author | Feng, Xin | |
dc.contributor.author | Zhang, Peiwen | |
dc.contributor.author | Han, Myong Hun | |
dc.contributor.author | You, Fang | |
dc.contributor.author | Yang, Yi | |
dc.contributor.author | Zhang, Wenlian | |
dc.contributor.author | Zheng, Wenyun | |
dc.date.accessioned | 2022-10-13T07:52:03Z | |
dc.date.available | 2022-10-13T07:52:03Z | |
dc.date.issued | 2021-05-01 | |
dc.identifier.citation | Nie, 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.issn | 0753-3322 | |
dc.identifier.uri | https://scholarbank.nus.edu.sg/handle/10635/233206 | |
dc.description.abstract | Tumor 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.publisher | Elsevier Masson s.r.l. | |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 International | |
dc.rights.uri | https://creativecommons.org/licenses/by-nc-nd/4.0/ | |
dc.source | Scopus OA2021 | |
dc.subject | Designing and constructing | |
dc.subject | Humanized TNF-?-specific Nb | |
dc.subject | Phage display library | |
dc.subject | Screening and identifyin | |
dc.subject | Single domain antibodies | |
dc.type | Article | |
dc.contributor.department | NUS ENVIRONMENTAL RESEARCH INSTITUTE | |
dc.description.doi | 10.1016/j.biopha.2021.111328 | |
dc.description.sourcetitle | Biomedicine and Pharmacotherapy | |
dc.description.volume | 137 | |
dc.description.page | 111328 | |
Appears in Collections: | Elements Staff Publications |
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