Controlling self-assembly of a peptide-based material via metal-ion induced registry shift

Paolo Anzini, Chunfu Xu, Spencer Hughes, Elizabeth Magnotti, Tao Jiang, Lars Hemmingsen, Borries Demeler, Vincent P. Conticello

Research output: Contribution to journalArticlepeer-review

39 Scopus citations

Abstract

Peptide TZ1C2 can populate two distinct orientations: a staggered (out-of-register) fibril and an aligned (in-register) coiled-coil trimer. The coordination of two cadmium ions induces a registry shift that results in a reversible transition between these structural forms. This process recapitulates the self-assembly mechanism of native protein fibrils in which a ligand binding event gates a reversible conformational transition between alternate forms of a folded peptide structure.

Original languageEnglish (US)
Pages (from-to)10278-10281
Number of pages4
JournalJournal of the American Chemical Society
Volume135
Issue number28
DOIs
StatePublished - Jul 17 2013

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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