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

Chang EP, Russ JA, Verch A, Kröger R, Estroff LA, Evans JS - Biochemistry (2014)

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: Laboratory for Chemical Physics, Department of Skeletal Biology, New York University , New York, New York 10012, United States.

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.

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(A) Representativecalcite crystals obtained from protein-deficientcontrols. (B and C) Representative nanoparticle assemblies generatedby AP7 in 1 h, revealing three-dimensional nanopatterning and buildingblock construction.Note the occurrence of gaps or spaces between nanoparticles in panelC.
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fig1: (A) Representativecalcite crystals obtained from protein-deficientcontrols. (B and C) Representative nanoparticle assemblies generatedby AP7 in 1 h, revealing three-dimensional nanopatterning and buildingblock construction.Note the occurrence of gaps or spaces between nanoparticles in panelC.

Mentions: In this work, we describe theadditional ability of C-RING AP7protein phases to modify calcite crystals in two dramatic ways. First,these protein phases direct the nucleation of highly oriented calcitenanoparticles on calcite crystals formed in standard calcium carbonatemineralization assays (Figure 1). The formationof these nanoparticles mimics the findings obtained in polymer phase-based7 and gel-based8 mineralizationsystems. Second, these surface nanoparticle assemblies and associatedgap regions become incorporated into the bulk crystal during overgrowth,leading to the introduction of nanoporosities within the bulk crystal(Figure 2). Thus, intracrystalline proteinphases, such as those generated by C-RING AP7, not only induce mineralassembly in solution4 but also can introducenew physical properties (i.e., nanopatterning and nanoporosities)into crystals.


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

Chang EP, Russ JA, Verch A, Kröger R, Estroff LA, Evans JS - Biochemistry (2014)

(A) Representativecalcite crystals obtained from protein-deficientcontrols. (B and C) Representative nanoparticle assemblies generatedby AP7 in 1 h, revealing three-dimensional nanopatterning and buildingblock construction.Note the occurrence of gaps or spaces between nanoparticles in panelC.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4215888&req=5

fig1: (A) Representativecalcite crystals obtained from protein-deficientcontrols. (B and C) Representative nanoparticle assemblies generatedby AP7 in 1 h, revealing three-dimensional nanopatterning and buildingblock construction.Note the occurrence of gaps or spaces between nanoparticles in panelC.
Mentions: In this work, we describe theadditional ability of C-RING AP7protein phases to modify calcite crystals in two dramatic ways. First,these protein phases direct the nucleation of highly oriented calcitenanoparticles on calcite crystals formed in standard calcium carbonatemineralization assays (Figure 1). The formationof these nanoparticles mimics the findings obtained in polymer phase-based7 and gel-based8 mineralizationsystems. Second, these surface nanoparticle assemblies and associatedgap regions become incorporated into the bulk crystal during overgrowth,leading to the introduction of nanoporosities within the bulk crystal(Figure 2). Thus, intracrystalline proteinphases, such as those generated by C-RING AP7, not only induce mineralassembly in solution4 but also can introducenew physical properties (i.e., nanopatterning and nanoporosities)into crystals.

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: Laboratory for Chemical Physics, Department of Skeletal Biology, New York University , New York, New York 10012, United States.

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.

Show MeSH