Controlling Self-Assembly of a Peptide-Based Material via Metal-Ion Induced Registry Shift

• Authors: Paolo Anzini, Emory University; Chunfu Xu, Emory University; Spencer Hughes, Emory University; Elizabeth Magnotti, Emory University; Tao Jiang, Emory University; Lars Hemmingsen, University of Copenhagen; Borries Demeler, The University of Texas; Vincent Conticello, Emory University
• Journal Title: Journal of the American Chemical Society
• Volume: Volume 135, Number 28
• Publisher: American Chemical Society | 2013-07-17, Pages 10278-10281
• Type of Work: Article | Post-print: After Peer Review
• Publisher DOI: http://doi.org/10.1021/ja404677c
• Subjects: Chemistry, General; Health Sciences, General; Chemistry, Biochemistry

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.