Acceleration of Calcite Kinetics by Abalone Nacre Proteins

Fu, Germaine; Qiu, Siyao; Orme, Christine A.; Morse, Daniel E.; Yoreo, James J. De

doi:10.1002/adma.200500633

Cited by 129 publications

(200 citation statements)

References 30 publications

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“…Table 1 shows that 0.1-M levels of the peptides containing as many as six aspartic acids enhanced growth by 0.5-15% over the control velocity. The v/v 0 values at 0.1 M for larger synthetic linear 27-mer peptides, (Asp 3 -Gly) 6 -Asp 3 and (Asp 3 -Ser) 6 -Asp 3 , showed much greater increases in step velocity of 64% and 44%, respectively.…”

Section: Resultsmentioning

confidence: 92%

“…It should be noted that step velocity data in these studies were obtained at slightly different supersaturation and ionic strength conditions (6,7). The most potent additive was AP8-␣, an 8-kDa, highly acidic protein extracted from the mineralized tissue of abalone (10).…”

Section: Resultsmentioning

confidence: 98%

“…To relate these findings for synthetic peptides to effects of native proteins, we also calculated interpolated values for (v/v 0 ) 0.1 M from the data obtained in the studies of Fu et al (6) and Kim et al (7). It should be noted that step velocity data in these studies were obtained at slightly different supersaturation and ionic strength conditions (6,7).…”

Section: Resultsmentioning

confidence: 99%

“…The widely accepted view of the latter mechanism is that macromolecular modifiers in solution are capable of directing growth morphology, but have only neutral or inhibitory effects on growth rate. Recently, this dogma was challenged by showing that low nanomolar levels of proteins isolated from abalone nacre actually increased rates of calcite growth by as much as 5-fold by accelerating the kinetics of molecular step propagation across mineral surfaces (6,7).…”

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confidence: 99%

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Role of molecular charge and hydrophilicity in regulating the kinetics of crystal growth

Elhadj

Yoreo

Hoyer

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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239

323

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The composition of biologic molecules isolated from biominerals suggests that control of mineral growth is linked to biochemical features. Here, we define a systematic relationship between the ability of biomolecules in solution to promote the growth of calcite (CaCO 3) and their net negative molecular charge and hydrophilicity. The degree of enhancement depends on peptide composition, but not on peptide sequence. Data analysis shows that this rate enhancement arises from an increase in the kinetic coefficient. We interpret the mechanism of growth enhancement to be a catalytic process whereby biomolecules reduce the magnitude of the diffusive barrier, E k, by perturbations that displace water molecules. The result is a decrease in the energy barrier for attachment of solutes to the solid phase. This previously unrecognized relationship also rationalizes recently reported data showing acceleration of calcite growth rates over rates measured in the pure system by nanomolar levels of abalone nacre proteins. These findings show that the growth-modifying properties of small model peptides may be scaled up to analyze mineralization processes that are mediated by more complex proteins. We suggest that enhancement of calcite growth may now be estimated a priori from the composition of peptide sequences and the calculated values of hydrophilicity and net molecular charge. This insight may contribute to an improved understanding of diverse systems of biomineralization and design of new synthetic growth modulators.biomineral ͉ calcite ͉ proteins

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Section: Resultsmentioning

confidence: 92%

Section: Resultsmentioning

confidence: 98%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Role of molecular charge and hydrophilicity in regulating the kinetics of crystal growth

Elhadj

Yoreo

Hoyer

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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239

323

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“…[71] This test has been performed with soluble matrices extracted from both calcite and aragonite. [72][73][74][75] The test was adapted as follows: different amounts of ASM (0.1 mg mL À1 to 20 mg mL À1 ) in CaCl 2 solution (10 mm, 500 mL) were introduced onto an 8-well culture slide (BD Falcon). The culture slide was closed with a plastic cover, which had been pierced with 1 mm holes.…”

Section: Methodsmentioning

confidence: 99%

Evolution of Nacre: Biochemistry and Proteomics of the Shell Organic Matrix of the Cephalopod Nautilus macromphalus

Marie¹,

Marin²,

Marie³

et al. 2009

ChemBioChem

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Matrix evolutions: We have biochemically characterized the nacre matrix of the cephalopod Nautilus macromphalus, in part by a proteomic approach applied to the acetic acid‐soluble and ‐insoluble shell matrices, as well as to spots obtained after 2D gel electrophoresis. Strikingly, most of the obtained partial sequences are entirely new, whereas a few correspond only partly with bivalvian nacre proteins. Our findings shed new light on the macroevolution of nacre matrix proteins. magnified imageIn mollusks, one of the most widely studied shell textures is nacre, the lustrous aragonitic layer that constitutes the internal components of the shells of several bivalves, a few gastropods, and one cephalopod: the nautilus. Nacre contains a minor organic fraction, which displays a wide range of functions in relation to the biomineralization process. Here, we have biochemically characterized the nacre matrix of the cephalopod Nautilus macromphalus. The acid‐soluble matrix contains a mixture of polydisperse and discrete proteins and glycoproteins, which interact with the formation of calcite crystals. In addition, a few bind calcium ions. Furthermore, we have used a proteomic approach, which was applied to the acetic acid‐soluble and ‐insoluble shell matrices, as well as to spots obtained after 2D gel electrophoresis. Our data demonstrate that the insoluble and soluble matrices, although different in their bulk monosaccharide and amino acid compositions, contain numerous shared peptides. Strikingly, most of the obtained partial sequences are entirely new. A few only partly match with bivalvian nacre proteins. Our findings have implications for knowledge of the long‐term evolution of molluskan nacre matrices.

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