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Heterogeneous nucleation of hydroxyapatite on protein: structural effect of silk sericin
Author(s) -
Akari Takeuchi,
Chikara Ohtsuki,
Toshiki Miyazaki,
Masanobu Kamitakahara,
Shinichi Ogata,
Masao Yamazaki,
Yoshiaki Furutani,
Hisao Kinoshita,
Masao Tanihara
Publication year - 2005
Publication title -
journal of the royal society interface
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.655
H-Index - 139
eISSN - 1742-5689
pISSN - 1742-5662
DOI - 10.1098/rsif.2005.0052
Subject(s) - biomineralization , nucleation , sericin , silk , chemical engineering , chemistry , protein crystallization , simulated body fluid , biophysics , calcium , metastability , octacalcium phosphate , deposition (geology) , apatite , materials science , crystallization , mineralogy , organic chemistry , composite material , engineering , paleontology , sediment , biology
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 β 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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