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Expression and purification of short hydrophobic elastin-like polypeptides with maltose-binding protein as a solubility tag

dc.contributor.authorBATAILLE, Laure
dc.contributor.authorDIERYCK, Wilfrid
dc.contributor.authorHOCQUELLET, Agnes
dc.contributor.authorCABANNE, Charlotte
dc.contributor.authorBATHANY, Katell
dc.contributor.authorLECOMMANDOUX, Sebastien
dc.contributor.authorGARBAY, Bertrand
ORCID: 0000-0001-5756-2627
IDREF: 033777551
dc.contributor.authorGARANGER, Elisabeth
IDREF: 089451740
dc.date.accessioned2020-09-03T07:56:05Z
dc.date.available2020-09-03T07:56:05Z
dc.date.issued2016
dc.identifier.issn1046-5928
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/10813
dc.description.abstractEnElastin-like polypeptides (ELPs) are biodegradable polymers with interesting physico-chemical properties for biomedical and biotechnological applications. The recombinant expression of hydrophobic elastin-like polypeptides is often difficult because they possess low transition temperatures, and therefore form aggregates at sub-ambient temperatures. To circumvent this difficulty, we expressed in Escherichia coli three hydrophobic ELPs (VPGIG)(n) with variable lengths (n = 20, 40, and 60) in fusion with the maltose-binding protein (MBP). Fusion proteins were soluble and yields of purified MBP-ELP ranged between 66 and 127 mg/L culture. After digestion of the fusion proteins by enterokinase, the ELF moiety was purified by using inverse transition cycling. The purified fraction containing ELP40 was slightly contaminated by traces of undigested fusion protein. Purification of ELP60 was impaired because of co-purification of the MBP tag during inverse transition cycling. ELP20 was successfully purified to homogeneity, as assessed by gel electrophoresis and mass spectrometry analyses. The transition temperature of ELP20 was measured at 15.4 degrees C in low salt buffer. In conclusion, this method can be used to produce hydrophobic ELF of low molecular mass. (C) 2015 Elsevier Inc. All rights reserved.
dc.language.isoen
dc.title.enExpression and purification of short hydrophobic elastin-like polypeptides with maltose-binding protein as a solubility tag
dc.typeArticle de revue
dc.subject.halChimie/Matériaux
bordeaux.journalProtein Expression and Purification
bordeaux.page165-171
bordeaux.volume110
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248*
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN, UMR 5248)
bordeaux.institutionUniversité de Bordeaux
bordeaux.institutionBordeaux INP
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Protein%20Expression%20and%20Purification&rft.date=2016&rft.volume=110&rft.spage=165-171&rft.epage=165-171&rft.eissn=1046-5928&rft.issn=1046-5928&rft.au=BATAILLE,%20Laure&DIERYCK,%20Wilfrid&HOCQUELLET,%20Agnes&CABANNE,%20Charlotte&BATHANY,%20Katell&rft.genre=article


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