TY - JOUR
T1 - Nacre protein fragment templates lamellar aragonite growth
AU - Metzler, Rebecca A.
AU - Evans, John Spencer
AU - Killian, Christopher E.
AU - Zhou, Dong
AU - Churchill, Tyler H.
AU - Appathurai, Narayana P.
AU - Coppersmith, Susan N.
AU - Gilbert, P. U.P.A.
PY - 2010/5/12
Y1 - 2010/5/12
N2 - 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.
AB - 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.
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U2 - 10.1021/ja909735y
DO - 10.1021/ja909735y
M3 - Article
C2 - 20397648
AN - SCOPUS:77952032298
SN - 0002-7863
VL - 132
SP - 6329
EP - 6334
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
IS - 18
ER -