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| Hauptseite > Publikationsdatenbank > Engineered aggregation inhibitor fusion for production of highly amyloidogenic human islet amyloid polypeptide > print |
| Hauptseite > Publikationsdatenbank > Engineered aggregation inhibitor fusion for production of highly amyloidogenic human islet amyloid polypeptide > print |
| 001 | 172157 | ||
| 005 | 20210129214400.0 | ||
| 024 | 7 | _ | |a 10.1016/j.jbiotec.2014.06.006 |2 doi |
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| 037 | _ | _ | |a FZJ-2014-05667 |
| 041 | _ | _ | |a ENG |
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| 100 | 1 | _ | |a Mirecka, Ewa Agnieszka |0 P:(DE-HGF)0 |b 0 |
| 245 | _ | _ | |a Engineered aggregation inhibitor fusion for production of highly amyloidogenic human islet amyloid polypeptide |
| 260 | _ | _ | |a Amsterdam [u.a.] |c 2014 |b Elsevier Science |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1415702490_21370 |2 PUB:(DE-HGF) |
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| 520 | _ | _ | |a Human islet amyloid polypeptide (IAPP) is the major component of pancreatic amyloid deposits in type 2 diabetes. The structural conversion of IAPP from a monomeric state into amyloid assemblies is the subject of intense research. Recombinant production of IAPP is, however, difficult due to its extreme aggregation propensity. Here we describe a novel strategy for expression of IAPP in Escherichia coli, based on an engineered protein tag, which sequesters IAPP monomers and prevents IAPP aggregation. The IAPP-binding protein HI18 was selected by phage display from a β-wrapin library. Fusion of HI18 to IAPP enabled the soluble expression of the construct. IAPP was cleaved from the fusion construct and purified to homogeneity with a yield of 3mg of isotopically labeled peptide per liter of culture. In the monomeric state, IAPP was largely disordered as evidenced by far-UV CD and liquid-state NMR spectroscopy but competent to form amyloid fibrils according to atomic force microscopy. These results demonstrate the ability of the engineered β-wrapin HI18 for shielding the hydrophobic sequence of IAPP during expression and purification. Fusion of aggregation-inhibiting β-wrapins is a suitable approach for the recombinant production of aggregation-prone proteins. |
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| 700 | 1 | _ | |a Schiefer, Stephanie |0 P:(DE-HGF)0 |b 2 |
| 700 | 1 | _ | |a Oesterhelt, Filipp |0 P:(DE-HGF)0 |b 3 |
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| 700 | 1 | _ | |a Hoyer, Wolfgang |0 P:(DE-HGF)0 |b 6 |e Corresponding Author |
| 773 | _ | _ | |a 10.1016/j.jbiotec.2014.06.006 |g p. S0168165614002879 |0 PERI:(DE-600)2016476-2 |p S0168-1656(14)00287-9 |t Journal of biotechnology |v - |y 2014 |x 0168-1656 |
| 856 | 4 | _ | |u http://www.sciencedirect.com/science/article/pii/S0168165614002879 |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/172157/files/FZJ-2014-05667.pdf |y Restricted |
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