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

doi:10.1021/ja404677c

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

Chemistry and Biochemistry

Research output: Contribution to journal › Article › peer-review

53 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 language	English
Pages (from-to)	10278-10281
Number of pages	4
Journal	Journal of the American Chemical Society
Volume	135
Issue number	28
DOIs	https://doi.org/10.1021/ja404677c
State	Published - Jul 17 2013

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10.1021/ja404677c

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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.",

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AU - Anzini, Paolo

AU - Xu, Chunfu

AU - Hughes, Spencer

AU - Magnotti, Elizabeth

AU - Jiang, Tao

AU - Hemmingsen, Lars

AU - Demeler, Borries

AU - Conticello, Vincent P.

PY - 2013/7/17

Y1 - 2013/7/17

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/84880374874

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IS - 28

ER -

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

Abstract

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