A study of the correlation between organic matrices and nanocomposite materials in oyster shell formation.
Calcium carbonate minerals are an integral part of many organisms. These biogenic minerals are all of original size, shape and high strength, and they are quite different from those found in their abiotic precipitates. It has been accepted that the formation, morphological development and crystallography of the biocomposites are controlled by the intrinsic molecular recognition of macromolecules. In this study, with the analyses of X-ray diffraction and scanning electron microscopy of the texture of biogenic minerals in oyster shells, we noted that the intracrystalline proteins deliberately reduce the coherence lengths of biogenic crystals compared to synthetic ones, leading to more isotropy. In order to understand the exact nature of the controlled nucleation and growth, we investigated the changes in protein conformation in vivo from the mineral-specific layers using Fourier self-deconvolution and Gaussian curve-fitting techniques. And via in vitro assays, we studied the relation of such changes to biomineral phase and morphology. We showed that the shell proteins in vivo are in the higher structural ordered state, and beta-antiparallel structure was predominant in each shell layer. Also, as the shell undergoes a change of calcium carbonate polymorphs from aragonite to calcite, significant alterations of the protein conformation with the denaturing of alpha-helix and beta-structure in the aragonitic layer is induced. These results provide a relationship between the effects of conformational changes on the nanostructure of biocomposites and the necessity of new synthetic strategies.
Choi
C S
CS
Department of Chemical Engineering, SoGang University, Seoul, South Korea. cschoi@ccs.sogang.ac.kr
Kim
Y W
YW
D000818:Animals; D002119:Calcium Carbonate / Q000737:chemistry*; D002850:Chromatography, Gel; D018360:Crystallography, X-Ray; D008855:Microscopy, Electron, Scanning; D010125:Ostreidae / Q000737:chemistry*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D017550:Spectroscopy, Fourier Transform Infrared
D011506:Proteins; D002119:Calcium Carbonate