Issue 58, 2018

Re-designing the α-synuclein tetramer

Abstract

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

Supplementary files

Article information

Article type
Communication
Submitted
21 May 2018
Accepted
27 Jun 2018
First published
02 Jul 2018

Chem. Commun., 2018,54, 8080-8083

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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