Re-designing the α-synuclein tetramer

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish (Ireland)
Pages (from-to)-
Number of pages4
JournalChemical Communications
Volume54
Issue number58
DOIs
Publication statusPublished - 2018

Fingerprint

Dive into the research topics of 'Re-designing the α-synuclein tetramer'. Together they form a unique fingerprint.

Cite this