The intrinsically disordered C-RING biomineralization protein, AP7, creates protein phases that introduce nanopatterning and nanoporosities into mineral crystals

Eric P. Chang, Jennie A. Russ, Andreas Verch, Roland Kröger, Lara A. Estroff, John Evans

Research output: Contribution to journalArticle

Abstract

We report an interesting process whereby the formation of nanoparticle assemblies on and nanoporosities within calcite crystals is directed by an intrinsically disordered C-RING mollusk shell nacre protein, AP7. Under mineralization conditions, AP7 forms protein phases that direct the nucleation of ordered calcite nanoparticles via a repetitive protein phase deposition process onto calcite crystals. These organized nanoparticles are separated by gaps or spaces that become incorporated into the forming bulk crystal as nanoporosities. This is an unusual example of organized nanoparticle biosynthesis and mineral modification directed by a C-RING protein phase.

Original languageEnglish (US)
Pages (from-to)4317-4319
Number of pages3
JournalBiochemistry
Volume53
Issue number27
DOIs
StatePublished - Jul 15 2014

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Biomineralization
Nanoparticles
Minerals
Calcium Carbonate
Crystals
Nacre
Proteins
Mollusca
Biosynthesis
Protein C
Nucleation

ASJC Scopus subject areas

  • Biochemistry

Cite this

The intrinsically disordered C-RING biomineralization protein, AP7, creates protein phases that introduce nanopatterning and nanoporosities into mineral crystals. / Chang, Eric P.; Russ, Jennie A.; Verch, Andreas; Kröger, Roland; Estroff, Lara A.; Evans, John.

In: Biochemistry, Vol. 53, No. 27, 15.07.2014, p. 4317-4319.

Research output: Contribution to journalArticle

Chang, Eric P. ; Russ, Jennie A. ; Verch, Andreas ; Kröger, Roland ; Estroff, Lara A. ; Evans, John. / The intrinsically disordered C-RING biomineralization protein, AP7, creates protein phases that introduce nanopatterning and nanoporosities into mineral crystals. In: Biochemistry. 2014 ; Vol. 53, No. 27. pp. 4317-4319.
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