There are no files associated with this item.
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.citation.endPage | 1398 | - |
dc.citation.number | 6 | - |
dc.citation.startPage | 1391 | - |
dc.citation.title | WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY | - |
dc.citation.volume | 27 | - |
dc.contributor.author | Maeng, Bo Hee | - |
dc.contributor.author | Nam, Dong Hyun | - |
dc.contributor.author | Kim, Yong Hwan | - |
dc.date.accessioned | 2023-12-22T06:08:38Z | - |
dc.date.available | 2023-12-22T06:08:38Z | - |
dc.date.created | 2016-09-06 | - |
dc.date.issued | 2011-06 | - |
dc.description.abstract | Molecular chaperones are a ubiquitous family of cellular proteins that mediate the correct folding of other target polypeptides. In our previous study, the recombinant anti-BNP scFv, which has promising applications for diagnostic, prognostic, and therapeutic monitoring of heart failure, was expressed in the cytoplasm of Escherichia coli. However, when the anti-BNP scFv was expressed, 73.4% of expressed antibodies formed insoluble inclusion bodies. In this study, molecular chaperones were coexpressed with anti-BNP scFv with the goal of improving the production of functional anti-BNP in the cytoplasm of E. coli. Five sets of molecular chaperones were assessed for their effects on the production of active anti-BNP scFv. These sets included the following: trigger factor (TF); groES/groEL; groES/groEL/TF; dnaK/dnaJ/grpE; groES/groEL/dnaK/dnaJ/grpE. Of these chaperones, the coexpression of anti-BNP scFv with the groES/groEL chaperones encoded in plasmid pGro7 exhibited the most efficient functional expression of anti-BNP scFv as an active form. Coexpressed with the groES/groEL chaperones, 64.9% of the total anti-BNP scFv was produced in soluble form, which is 2.4 times higher scFv than that of anti-BNP scFv expressed without molecular chaperones, and the relative binding activity was 1.5-fold higher. The optimal concentration of l-arabinose required for induction of the groES/groEL chaperone set was determined to be 1.0 mM and relative binding activity was 3.5 times higher compared with that of no induction with l-arabinose. In addition, soluble anti-BNP scFv was increased from 11.5 to 31.4 mu g/ml with optimized inducer concentration (1.0 mM l-arabinose) for the coexpression of the groES/groEL chaperones. These results demonstrate that the functional expression of anti-BNP scFv can be improved by coexpression of molecular chaperones, as molecular chaperones can identify and help to refold improperly folded anti-BNP scFv | - |
dc.identifier.bibliographicCitation | WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY, v.27, no.6, pp.1391 - 1398 | - |
dc.identifier.doi | 10.1007/s11274-010-0590-5 | - |
dc.identifier.issn | 0959-3993 | - |
dc.identifier.scopusid | 2-s2.0-79955793446 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/20372 | - |
dc.identifier.url | http://link.springer.com/article/10.1007%2Fs11274-010-0590-5 | - |
dc.identifier.wosid | 000290320900014 | - |
dc.language | 영어 | - |
dc.publisher | SPRINGER | - |
dc.title | Coexpression of molecular chaperones to enhance functional expression of anti-BNP scFv in the cytoplasm of Escherichia coli for the detection of B-type natriuretic peptide | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
Items in Repository are protected by copyright, with all rights reserved, unless otherwise indicated.
Tel : 052-217-1404 / Email : scholarworks@unist.ac.kr
Copyright (c) 2023 by UNIST LIBRARY. All rights reserved.
ScholarWorks@UNIST was established as an OAK Project for the National Library of Korea.