Calcium-Induced Molecular Rearrangement of Peptide Folds Enables Biomineralization of Vaterite Calcium Carbonate

Hao Lu; Helmut Lutz; Steven J. Roeters; Matthew A. Hood; Arne Schäfer; Rafael MunÌoz-Espí; Rüdiger Berger; Mischa Bonn; Tobias Weidner

doi:10.1021/jacs.8b00281

Calcium-Induced Molecular Rearrangement of Peptide Folds Enables Biomineralization of Vaterite Calcium Carbonate

Hao Lu^*, Helmut Lutz, Steven J. Roeters, Matthew A. Hood, Arne Schäfer, Rafael MunÌoz-Espí, Rüdiger Berger, Mischa Bonn, Tobias Weidner

^*Corresponding author for this work

Department of Chemistry

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

49 Citations (Scopus)

Abstract

Proteins can control mineralization of CaCO₃ by selectively triggering the growth of calcite, aragonite or vaterite phases. The templating of CaCO₃ by proteins must occur predominantly at the protein/CaCO₃ interface, yet molecular-level insights into the interface during active mineralization have been lacking. Here, we investigate the role of peptide folding and structural flexibility on the mineralization of CaCO₃. We study two amphiphilic peptides based on glutamic acid and leucine with β-sheet and α-helical structures. Though both sequences lead to vaterite structures, the β-sheets yield free-standing vaterite nanosheet with superior stability and purity. Surface-spectroscopy and molecular dynamics simulations reveal that reciprocal structuring of calcium ions and peptides lead to the effective synthesis of vaterite by mimicry of the (001) crystal plane.

Original language	English
Journal	Journal of the American Chemical Society
Volume	140
Issue	8
Pages (from-to)	2793-2796
Number of pages	4
ISSN	0002-7863
DOIs	https://doi.org/10.1021/jacs.8b00281
Publication status	Published - 28 Feb 2018

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title = "Calcium-Induced Molecular Rearrangement of Peptide Folds Enables Biomineralization of Vaterite Calcium Carbonate",

abstract = "Proteins can control mineralization of CaCO3 by selectively triggering the growth of calcite, aragonite or vaterite phases. The templating of CaCO3 by proteins must occur predominantly at the protein/CaCO3 interface, yet molecular-level insights into the interface during active mineralization have been lacking. Here, we investigate the role of peptide folding and structural flexibility on the mineralization of CaCO3. We study two amphiphilic peptides based on glutamic acid and leucine with β-sheet and α-helical structures. Though both sequences lead to vaterite structures, the β-sheets yield free-standing vaterite nanosheet with superior stability and purity. Surface-spectroscopy and molecular dynamics simulations reveal that reciprocal structuring of calcium ions and peptides lead to the effective synthesis of vaterite by mimicry of the (001) crystal plane.",

author = "Hao Lu and Helmut Lutz and Roeters, {Steven J.} and Hood, {Matthew A.} and Arne Sch{\"a}fer and Rafael Mun{\`I}oz-Esp{\'i} and R{\"u}diger Berger and Mischa Bonn and Tobias Weidner",

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Calcium-Induced Molecular Rearrangement of Peptide Folds Enables Biomineralization of Vaterite Calcium Carbonate. / Lu, Hao; Lutz, Helmut; Roeters, Steven J. et al.
In: Journal of the American Chemical Society, Vol. 140, No. 8, 28.02.2018, p. 2793-2796.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

TY - JOUR

T1 - Calcium-Induced Molecular Rearrangement of Peptide Folds Enables Biomineralization of Vaterite Calcium Carbonate

AU - Lu, Hao

AU - Lutz, Helmut

AU - Roeters, Steven J.

AU - Hood, Matthew A.

AU - Schäfer, Arne

AU - MunÌoz-Espí, Rafael

AU - Berger, Rüdiger

AU - Bonn, Mischa

AU - Weidner, Tobias

PY - 2018/2/28

Y1 - 2018/2/28

N2 - Proteins can control mineralization of CaCO3 by selectively triggering the growth of calcite, aragonite or vaterite phases. The templating of CaCO3 by proteins must occur predominantly at the protein/CaCO3 interface, yet molecular-level insights into the interface during active mineralization have been lacking. Here, we investigate the role of peptide folding and structural flexibility on the mineralization of CaCO3. We study two amphiphilic peptides based on glutamic acid and leucine with β-sheet and α-helical structures. Though both sequences lead to vaterite structures, the β-sheets yield free-standing vaterite nanosheet with superior stability and purity. Surface-spectroscopy and molecular dynamics simulations reveal that reciprocal structuring of calcium ions and peptides lead to the effective synthesis of vaterite by mimicry of the (001) crystal plane.

AB - Proteins can control mineralization of CaCO3 by selectively triggering the growth of calcite, aragonite or vaterite phases. The templating of CaCO3 by proteins must occur predominantly at the protein/CaCO3 interface, yet molecular-level insights into the interface during active mineralization have been lacking. Here, we investigate the role of peptide folding and structural flexibility on the mineralization of CaCO3. We study two amphiphilic peptides based on glutamic acid and leucine with β-sheet and α-helical structures. Though both sequences lead to vaterite structures, the β-sheets yield free-standing vaterite nanosheet with superior stability and purity. Surface-spectroscopy and molecular dynamics simulations reveal that reciprocal structuring of calcium ions and peptides lead to the effective synthesis of vaterite by mimicry of the (001) crystal plane.

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SN - 0002-7863

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ER -

Calcium-Induced Molecular Rearrangement of Peptide Folds Enables Biomineralization of Vaterite Calcium Carbonate

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