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. 2005 Sep 22;2(4):373-8.
doi: 10.1098/rsif.2005.0052.

Heterogeneous nucleation of hydroxyapatite on protein: structural effect of silk sericin

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Heterogeneous nucleation of hydroxyapatite on protein: structural effect of silk sericin

Akari Takeuchi et al. J R Soc Interface. .

Abstract

Acidic proteins play an important role during mineral formation in biological systems, but the mechanism of mineral formation is far from understood. In this paper, we report on the relationship between the structure of a protein and hydroxyapatite deposition under biomimetic conditions. Sericin, a type of silk protein, was adopted as a suitable protein for studying structural effect on hydroxyapatite deposition, since it forms a hydroxyapatite layer on its surface in a metastable calcium phosphate solution, and its structure has been reported. Sericin effectively induced hydroxyapatite nucleation when it has high molecular weight and a beta sheet structure. This indicates that the specific structure of a protein can effectively induce heterogeneous nucleation of hydroxyapatite in a biomimetic solution, i.e. a metastable calcium phosphate solution. This finding is useful in understanding biomineralization, as well as for the design of organic polymers that can effectively induce hydroxyapatite nucleation.

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Figures

Figure 1
Figure 1
GPC profiles of sericin samples prepared under various conditions.
Figure 2
Figure 2
CD spectra of the extracted sericin prepared under various conditions.
Figure 3
Figure 3
FT-IR spectra of sericin films prepared from various solutions.
Figure 4
Figure 4
SEM images of the surfaces of sericin films prepared from various solutions after soaking in the 1.5SBF for 7 days.
Figure 5
Figure 5
XRF spectrum of the surface of sample S105-2w after soaking in the 1.5SBF for 7 days.
Figure 6
Figure 6
TF-XRD patterns of sericin films prepared from various solutions after soaking in the 1.5SBF for 7 days.
Figure 7
Figure 7
Mechanism of hydroxyapatite nucleation on a polypeptide substrate with a β sheet structure in a highly saturated SBF.

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