On Biomineralization : Enzymes Switch on Mesocrystal Assembly

Rao, Ashit; Roncal-Herrero, Teresa; Schmid, Elina; Drechsler, Markus; Scheffner, Martin; Gebauer, Denis; Kröger, Roland; Cölfen, Helmut

On Biomineralization : Enzymes Switch on Mesocrystal Assembly

Dateien

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Datum

2019

Autor:innen

Rao, Ashit

Roncal-Herrero, Teresa

Schmid, Elina

Drechsler, Markus

Scheffner, Martin

Gebauer, Denis

Kröger, Roland

Cölfen, Helmut

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

ACS Central Science. 2019, 5(2), pp. 357-364. ISSN 2374-7943. eISSN 2374-7951. Available under: doi: 10.1021/acscentsci.8b00853

Zusammenfassung

Cellular machineries guide the bottom-up pathways toward crystal superstructures based on the transport of inorganic precursors and their precise integration with organic frameworks. The biosynthesis of mesocrystalline spines entails concerted interactions between biomolecules and inorganic precursors; however, the bioinorganic interactions and interfaces that regulate material form and growth as well as the selective emergence of structural complexity in the form of nanostructured crystals are not clear. By investigating mineral nucleation under the regulation of recombinant proteins, we show that SpSM50, a matrix protein of the sea urchin spine, stabilizes mineral precursors via vesicle-confinement, a function conferred by a low-complexity, disordered region. Site-specific proteolysis of this domain by a collagenase initiates phase transformation of the confined mineral phase. The residual C-type lectin domain molds the fluidic mineral precursor into hierarchical mesocrystals identical to structural crystal modules constituting the biogenic mineral. Thus, the regulatory functions of proteolytic enzymes can guide biomacromolecular domain constitutions and interfaces, in turn determining inorganic phase transformations toward hybrid materials as well as integrating organic and inorganic components across hierarchical length scales. Bearing striking resemblance to biogenic mineralization, these hybrid materials recruit bioinorganic interactions which elegantly intertwine nucleation and crystallization phenomena with biomolecular structural dynamics, hence elucidating a long-sought key of how nature can orchestrate complex biomineralization processes.

Fachgebiet (DDC)

540 Chemie

Zitieren

ISO 690

RAO, Ashit, Teresa RONCAL-HERRERO, Elina SCHMID, Markus DRECHSLER, Martin SCHEFFNER, Denis GEBAUER, Roland KRÖGER, Helmut CÖLFEN, 2019. On Biomineralization : Enzymes Switch on Mesocrystal Assembly. In: ACS Central Science. 2019, 5(2), pp. 357-364. ISSN 2374-7943. eISSN 2374-7951. Available under: doi: 10.1021/acscentsci.8b00853

BibTex

@article{Rao2019-02-27Biomi-44871,
  year={2019},
  doi={10.1021/acscentsci.8b00853},
  title={On Biomineralization : Enzymes Switch on Mesocrystal Assembly},
  number={2},
  volume={5},
  issn={2374-7943},
  journal={ACS Central Science},
  pages={357--364},
  author={Rao, Ashit and Roncal-Herrero, Teresa and Schmid, Elina and Drechsler, Markus and Scheffner, Martin and Gebauer, Denis and Kröger, Roland and Cölfen, Helmut}
}

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