Intrinsically disordered mollusk shell prismatic protein that modulates calcium carbonate crystal growth

Moise Ndao, Ellen Keene, Fairland F. Amos, Gita Rewari, Christopher B. Ponce, Lara Estroff, John Evans

Research output: Contribution to journalArticle

Abstract

The formation of calcite prism architecture in the prismatic layer of the mollusk shell involves the participation of a number of different proteins. One protein family, Asprich, has been identified as a participant in amorphous calcium carbonate stabilization and calcite architecture in the prismatic layer of the mollusk, Atrina rigida. However, the functional role(s) of this protein family are not fully understood due to the fact that insufficient quantities of these proteins are available for experimentation. To overcome this problem, we employed stepwise solid-phase synthesis to recreate one of the 10 members of the Asprich family, the 61 AA single chain protein, Asprich 3. We find that the Asprich 3 protein inhibits the formation of rhombohedral calcite crystals and induces the formation of round calcium carbonate deposits in vitro that contain calcite and amorphous calcium carbonate (ACC). This mineralization behavior does not occur under control conditions, and the formation of ACC and calcite is similar to that reported for the recombinant form of the Asprich g protein. Circular dichroism studies reveal that Asprich 3 is an intrinsically disordered protein, predominantly random coil (66%), with 20-30% β-strand content, a small percentage of β-turn, and little if any α-helical content. This protein is not extrinsically stabilized by Ca(II) ions but can be stabilized by 2,2,2-trifluoroethanol to form a structure consisting of turn-like and random coil characteristics. This finding suggests that Asprich 3 may require other extrinsic interactions (i.e., with mineral or ionic clusters or other macromolecules) to achieve folding. In conclusion, Asprich 3 possesses in vitro functional and structural qualities that are similar to other reported for other Asprich protein sequences.

Original languageEnglish (US)
Pages (from-to)2539-2544
Number of pages6
JournalBiomacromolecules
Volume11
Issue number10
DOIs
StatePublished - Oct 11 2010

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Calcium Carbonate
Calcium carbonate
Crystallization
Crystal growth
Proteins
Calcite
Intrinsically Disordered Proteins
Trifluoroethanol
Prisms
Macromolecules
Dichroism
Minerals
Deposits
Stabilization
Ions
Crystals

ASJC Scopus subject areas

  • Bioengineering
  • Materials Chemistry
  • Polymers and Plastics
  • Biomaterials

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Intrinsically disordered mollusk shell prismatic protein that modulates calcium carbonate crystal growth. / Ndao, Moise; Keene, Ellen; Amos, Fairland F.; Rewari, Gita; Ponce, Christopher B.; Estroff, Lara; Evans, John.

In: Biomacromolecules, Vol. 11, No. 10, 11.10.2010, p. 2539-2544.

Research output: Contribution to journalArticle

Ndao, Moise ; Keene, Ellen ; Amos, Fairland F. ; Rewari, Gita ; Ponce, Christopher B. ; Estroff, Lara ; Evans, John. / Intrinsically disordered mollusk shell prismatic protein that modulates calcium carbonate crystal growth. In: Biomacromolecules. 2010 ; Vol. 11, No. 10. pp. 2539-2544.
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