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

Akari Takeuchi, Chikara Ohtsuki, Toshiki Miyazaki, Masanobu Kamitakahara, Shin Ichi Ogata, Masao Yamazaki, Yoshiaki Furutani, Hisao Kinoshita, Masao Tanihara

Research output: Contribution to journalArticlepeer-review

112 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)373-378
Number of pages6
JournalJournal of the Royal Society Interface
Issue number4
Publication statusPublished - 2005


  • Biomimetic process
  • Biomineralization
  • Hydroxyapatite
  • Metastable calcium phosphate solution
  • Silk protein


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