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| Hauptseite > Publikationsdatenbank > Impact of subunit linkages in an engineered homodimeric binding protein to α-synuclein > print |
| Hauptseite > Publikationsdatenbank > Impact of subunit linkages in an engineered homodimeric binding protein to α-synuclein > print |
| 001 | 172156 | ||
| 005 | 20210129214400.0 | ||
| 024 | 7 | _ | |a 10.1093/protein/gzu047 |2 doi |
| 024 | 7 | _ | |a WOS:000345837300002 |2 WOS |
| 037 | _ | _ | |a FZJ-2014-05666 |
| 041 | _ | _ | |a English |
| 082 | _ | _ | |a 540 |
| 100 | 1 | _ | |a Gauhar, Aziz |0 P:(DE-HGF)0 |b 0 |
| 245 | _ | _ | |a Impact of subunit linkages in an engineered homodimeric binding protein to α-synuclein |
| 260 | _ | _ | |a Oxford |c 2014 |b Oxford Univ. Press |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1416228091_11277 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a article |2 DRIVER |
| 520 | _ | _ | |a Aggregation of the protein α-synuclein (α-syn) has been implicated in Parkinson's disease and other neurodegenerative disorders, collectively referred to as synucleinopathies. The β-wrapin AS69 is a small engineered binding protein to α-syn that stabilizes a β-hairpin conformation of monomeric α-syn and inhibits α-syn aggregation at substoichiometric concentrations. AS69 is a homodimer whose subunits are linked via a disulfide bridge between their single cysteine residues, Cys-28. Here we show that expression of a functional dimer as a single polypeptide chain is achievable by head-to-tail linkage of AS69 subunits. Choice of a suitable linker is essential for construction of head-to-tail dimers that exhibit undiminished α-syn affinity compared with the solely disulfide-linked dimer. We characterize AS69-GS3, a head-to-tail dimer with a glycine-serine-rich linker, under oxidized and reduced conditions in order to evaluate the impact of the Cys28-disulfide bond on structure, stability and α-syn binding. Formation of the disulfide bond causes compaction of AS69-GS3, increases its thermostability, and is a prerequisite for high-affinity binding to α-syn. Comparison of AS69-GS3 and AS69 demonstrates that head-to-tail linkage promotes α-syn binding by affording accelerated disulfide bond formation. |
| 536 | _ | _ | |a 453 - Physics of the Cell (POF2-453) |0 G:(DE-HGF)POF2-453 |c POF2-453 |f POF II |x 0 |
| 700 | 1 | _ | |a Shaykhalishahi, Hamed |0 P:(DE-HGF)0 |b 1 |
| 700 | 1 | _ | |a Gremer, Lothar |0 P:(DE-Juel1)145165 |b 2 |
| 700 | 1 | _ | |a Mirecka, Ewa |0 P:(DE-HGF)0 |b 3 |
| 700 | 1 | _ | |a Hoyer, Wolfgang |0 P:(DE-HGF)0 |b 4 |
| 773 | _ | _ | |a 10.1093/protein/gzu047 |0 PERI:(DE-600)1466729-0 |n 12 |p 473-479 |t Protein engineering design and selection |v 27 |y 2014 |x 0269-2139 |
| 856 | 4 | _ | |u http://peds.oxfordjournals.org/content/early/2014/10/20/protein.gzu047.long |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/172156/files/FZJ-2014-05666.pdf |y Restricted |
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| 914 | 1 | _ | |y 2014 |
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