Nacre protein fragment templates lamellar aragonite growth

Rebecca A. Metzler, John Spencer Evans, Christopher E. Killian, Dong Zhou, Tyler H. Churchill, Narayana P. Appathurai, Susan N. Coppersmith, P. U.P.A. Gilbert

    Research output: Contribution to journalArticlepeer-review


    Proteins play a major role in the formation of all biominerals. In mollusk shell nacre, complex mixtures and assemblies of proteins and polysaccharides were shown to induce aragonite formation, rather than the thermodynamically favored calcite (both aragonite and calcite are CaCO3 polymorphs). Here we used N16N, a single 30 amino acid-protein fragment originally inspired by the mineral binding site of N16, a protein in the nacre layer of the Japanese pearl oysters (Pinctada fucata). In a calcite growth solution this short peptide induces in vitro biomineralization. This model biomineral was analyzed using X-ray PhotoElectron Emission spectroMicroscopy (X-PEEM) and found to be strikingly similar to natural nacre: lamellar aragonite with interspersed N16N layers. This and other findings combined suggest a hypothetical scenario in which in vivo three proteins (N16, Pif80, and Pif97) and a polysaccharide (chitin) work in concert to form lamellar nacre.

    Original languageEnglish (US)
    Pages (from-to)6329-6334
    Number of pages6
    JournalJournal of the American Chemical Society
    Issue number18
    StatePublished - May 12 2010

    ASJC Scopus subject areas

    • Catalysis
    • General Chemistry
    • Biochemistry
    • Colloid and Surface Chemistry


    Dive into the research topics of 'Nacre protein fragment templates lamellar aragonite growth'. Together they form a unique fingerprint.

    Cite this