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Issue 58, 2018
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Re-designing the α-synuclein tetramer

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A computationally re-designed molecular loop optimizes helical packing of α-synuclein monomers to seal the aggregation-resistant low-weight tetramer, a key target for Parkinson's disease. Helical monomers are pushed into active conformations during supramolecular assembly, and familial missense mutations double the energy barrier to tetramerization, preserving the pool of potentially amyloidogenic monomers.

Graphical abstract: Re-designing the α-synuclein tetramer

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The article was received on 21 May 2018, accepted on 27 Jun 2018 and first published on 02 Jul 2018

Article type: Communication
DOI: 10.1039/C8CC04054K
Chem. Commun., 2018,54, 8080-8083

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    Re-designing the α-synuclein tetramer

    L. Xu, S. Bhattacharya and D. Thompson, Chem. Commun., 2018, 54, 8080
    DOI: 10.1039/C8CC04054K

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