Nacre protein sequence compartmentalizes mineral polymorphs in solution

Jong Seto, Andreas Picker, Yong Chen, Ashit Rao, John Evans, Helmut Cölfen

Research output: Contribution to journalArticle

Abstract

The Japanese pearl oyster (Pinctada fucata) n16 framework matrix protein is an integral part of the growth and formation of the mollusk shell biomineralization mechanism. It is a required component of the extracellular matrix with a dual mineralization role, as an anchor component to synchronize the assembly of the beta-chitin and N-series, Pif-series protein extracellular matrix for aragonite formation and as a regulator of aragonite formation itself. However, the mechanism by which this protein controls aragonite formation is not understood. Here, we investigate the mineralization potential and kinetics of the 30 AA N-terminal portion of the n16 protein, n16N. This sequence has been demonstrated to form either vaterite or aragonite depending upon conditions. Using in situ potentiometric titration methods, we find that n16N is indeed responsible for the self-assembly characteristics found in vivo and in vitro but is not involved with active Ca2+ binding or mineral nucleation processes. Upon the basis of time- and peptide concentration-dependent sampling of mineral deposits that form in solution, we find that n16N is responsible for controlling where mineralization occurs in bulk solution. This protein sequence acts as a molecular spacer that organizes the mineralization space and promotes the formation of mineral constituents that contain ACC, vaterite, and aragonite. Without the concerted action of the n16N assemblage, unregulated calcite formation occurs exclusively. Thus, the n16 protein provides the regulation needed to have the characteristic polymorph, crystalline orientations, and related mechanical properties associated to the microstructure of mollusk shells.

Original languageEnglish (US)
Pages (from-to)1501-1505
Number of pages5
JournalCrystal Growth and Design
Volume14
Issue number4
DOIs
StatePublished - Apr 2 2014

Fingerprint

Nacre
Calcium Carbonate
aragonite
Polymorphism
Minerals
minerals
proteins
Proteins
mollusks
matrices
chitin
Biomineralization
mineral deposits
Chitin
Mineral resources
regulators
Calcite
calcite
Anchors
Titration

ASJC Scopus subject areas

  • Chemistry(all)
  • Materials Science(all)
  • Condensed Matter Physics

Cite this

Nacre protein sequence compartmentalizes mineral polymorphs in solution. / Seto, Jong; Picker, Andreas; Chen, Yong; Rao, Ashit; Evans, John; Cölfen, Helmut.

In: Crystal Growth and Design, Vol. 14, No. 4, 02.04.2014, p. 1501-1505.

Research output: Contribution to journalArticle

Seto, Jong ; Picker, Andreas ; Chen, Yong ; Rao, Ashit ; Evans, John ; Cölfen, Helmut. / Nacre protein sequence compartmentalizes mineral polymorphs in solution. In: Crystal Growth and Design. 2014 ; Vol. 14, No. 4. pp. 1501-1505.
@article{886895797cb44a11b74e55499a78158f,
title = "Nacre protein sequence compartmentalizes mineral polymorphs in solution",
abstract = "The Japanese pearl oyster (Pinctada fucata) n16 framework matrix protein is an integral part of the growth and formation of the mollusk shell biomineralization mechanism. It is a required component of the extracellular matrix with a dual mineralization role, as an anchor component to synchronize the assembly of the beta-chitin and N-series, Pif-series protein extracellular matrix for aragonite formation and as a regulator of aragonite formation itself. However, the mechanism by which this protein controls aragonite formation is not understood. Here, we investigate the mineralization potential and kinetics of the 30 AA N-terminal portion of the n16 protein, n16N. This sequence has been demonstrated to form either vaterite or aragonite depending upon conditions. Using in situ potentiometric titration methods, we find that n16N is indeed responsible for the self-assembly characteristics found in vivo and in vitro but is not involved with active Ca2+ binding or mineral nucleation processes. Upon the basis of time- and peptide concentration-dependent sampling of mineral deposits that form in solution, we find that n16N is responsible for controlling where mineralization occurs in bulk solution. This protein sequence acts as a molecular spacer that organizes the mineralization space and promotes the formation of mineral constituents that contain ACC, vaterite, and aragonite. Without the concerted action of the n16N assemblage, unregulated calcite formation occurs exclusively. Thus, the n16 protein provides the regulation needed to have the characteristic polymorph, crystalline orientations, and related mechanical properties associated to the microstructure of mollusk shells.",
author = "Jong Seto and Andreas Picker and Yong Chen and Ashit Rao and John Evans and Helmut C{\"o}lfen",
year = "2014",
month = "4",
day = "2",
doi = "10.1021/cg401421h",
language = "English (US)",
volume = "14",
pages = "1501--1505",
journal = "Crystal Growth and Design",
issn = "1528-7483",
publisher = "American Chemical Society",
number = "4",

}

TY - JOUR

T1 - Nacre protein sequence compartmentalizes mineral polymorphs in solution

AU - Seto, Jong

AU - Picker, Andreas

AU - Chen, Yong

AU - Rao, Ashit

AU - Evans, John

AU - Cölfen, Helmut

PY - 2014/4/2

Y1 - 2014/4/2

N2 - The Japanese pearl oyster (Pinctada fucata) n16 framework matrix protein is an integral part of the growth and formation of the mollusk shell biomineralization mechanism. It is a required component of the extracellular matrix with a dual mineralization role, as an anchor component to synchronize the assembly of the beta-chitin and N-series, Pif-series protein extracellular matrix for aragonite formation and as a regulator of aragonite formation itself. However, the mechanism by which this protein controls aragonite formation is not understood. Here, we investigate the mineralization potential and kinetics of the 30 AA N-terminal portion of the n16 protein, n16N. This sequence has been demonstrated to form either vaterite or aragonite depending upon conditions. Using in situ potentiometric titration methods, we find that n16N is indeed responsible for the self-assembly characteristics found in vivo and in vitro but is not involved with active Ca2+ binding or mineral nucleation processes. Upon the basis of time- and peptide concentration-dependent sampling of mineral deposits that form in solution, we find that n16N is responsible for controlling where mineralization occurs in bulk solution. This protein sequence acts as a molecular spacer that organizes the mineralization space and promotes the formation of mineral constituents that contain ACC, vaterite, and aragonite. Without the concerted action of the n16N assemblage, unregulated calcite formation occurs exclusively. Thus, the n16 protein provides the regulation needed to have the characteristic polymorph, crystalline orientations, and related mechanical properties associated to the microstructure of mollusk shells.

AB - The Japanese pearl oyster (Pinctada fucata) n16 framework matrix protein is an integral part of the growth and formation of the mollusk shell biomineralization mechanism. It is a required component of the extracellular matrix with a dual mineralization role, as an anchor component to synchronize the assembly of the beta-chitin and N-series, Pif-series protein extracellular matrix for aragonite formation and as a regulator of aragonite formation itself. However, the mechanism by which this protein controls aragonite formation is not understood. Here, we investigate the mineralization potential and kinetics of the 30 AA N-terminal portion of the n16 protein, n16N. This sequence has been demonstrated to form either vaterite or aragonite depending upon conditions. Using in situ potentiometric titration methods, we find that n16N is indeed responsible for the self-assembly characteristics found in vivo and in vitro but is not involved with active Ca2+ binding or mineral nucleation processes. Upon the basis of time- and peptide concentration-dependent sampling of mineral deposits that form in solution, we find that n16N is responsible for controlling where mineralization occurs in bulk solution. This protein sequence acts as a molecular spacer that organizes the mineralization space and promotes the formation of mineral constituents that contain ACC, vaterite, and aragonite. Without the concerted action of the n16N assemblage, unregulated calcite formation occurs exclusively. Thus, the n16 protein provides the regulation needed to have the characteristic polymorph, crystalline orientations, and related mechanical properties associated to the microstructure of mollusk shells.

UR - http://www.scopus.com/inward/record.url?scp=84897559757&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84897559757&partnerID=8YFLogxK

U2 - 10.1021/cg401421h

DO - 10.1021/cg401421h

M3 - Article

VL - 14

SP - 1501

EP - 1505

JO - Crystal Growth and Design

JF - Crystal Growth and Design

SN - 1528-7483

IS - 4

ER -