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

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.

SUBMITTER: Anzini P

PROVIDER: S-EPMC3786573 | biostudies-other | 2013 Jul

REPOSITORIES: biostudies-other

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

Anzini Paolo P Xu Chunfu C Hughes Spencer S Magnotti Elizabeth E Jiang Tao T Hemmingsen Lars L Demeler Borries B Conticello Vincent P VP

Journal of the American Chemical Society 20130709 28

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. ...[more]

PMID: 23815081

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