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000279291 1001_ $$0P:(DE-Juel1)167315$$aShaykhalishahi, Hamed$$b0$$ufzj
000279291 245__ $$aContact between the β1 and β2 Segments of α-Synuclein that Inhibits Amyloid Formation
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000279291 520__ $$aConversion of the intrinsically disordered protein α-synuclein (α-syn) into amyloid aggregates is a key process in Parkinson’s disease. The sequence region 35–59 contains β-strand segments β1 and β2 of α-syn amyloid fibril models and most disease-related mutations. β1 and β2 frequently engage in transient interactions in monomeric α-syn. The consequences of β1–β2 contacts are evaluated by disulfide engineering, biophysical techniques, and cell viability assays. The double-cysteine mutant α-synCC, with a disulfide linking β1 and β2, is aggregation-incompetent and inhibits aggregation and toxicity of wild-type α-syn. We show that α-syn delays the aggregation of amyloid-β peptide and islet amyloid polypeptide involved in Alzheimer’s disease and type 2 diabetes, an effect enhanced in the α-synCC mutant. Tertiary interactions in the β1–β2 region of α-syn interfere with the nucleation of amyloid formation, suggesting promotion of such interactions as a potential therapeutic approach.
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000279291 7001_ $$0P:(DE-HGF)0$$aGauhar, Aziz$$b1
000279291 7001_ $$0P:(DE-HGF)0$$aWördehoff, Michael M.$$b2
000279291 7001_ $$0P:(DE-HGF)0$$aGrüning, Clara S. R.$$b3
000279291 7001_ $$0P:(DE-Juel1)145785$$aKlein, Antonia N.$$b4$$ufzj
000279291 7001_ $$0P:(DE-Juel1)157832$$aBannach, Oliver$$b5$$ufzj
000279291 7001_ $$0P:(DE-Juel1)132023$$aStoldt, Matthias$$b6$$ufzj
000279291 7001_ $$0P:(DE-Juel1)132029$$aWillbold, Dieter$$b7$$ufzj
000279291 7001_ $$0P:(DE-HGF)0$$aHärd, Torleif$$b8
000279291 7001_ $$0P:(DE-Juel1)166306$$aHoyer, Wolfgang$$b9$$eCorresponding author$$ufzj
000279291 773__ $$0PERI:(DE-600)2011836-3$$a10.1002/anie.201503018$$gVol. 54, no. 30, p. 8837 - 8840$$n30$$p8837 - 8840$$tAngewandte Chemie / International edition$$v54$$x1433-7851$$y2015
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