|
Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Environmental Science / Faculty of Environmental Earth Science >
Peer-reviewed Journal Articles, etc >
Binding of collagen gene products with titanium oxide
| Title: | Binding of collagen gene products with titanium oxide |
| Authors: | Song, Qin Browse this author | | Iku, Shouhei Browse this author | | Sammons, Rachel Browse this author | | Yagami, Kimitoshi Browse this author →KAKEN DB | | Furusawa, Toshitake Browse this author | | Morimoto, Koichi Browse this author →KAKEN DB | | Rahaman, Md Shiblur Browse this author | | Kurasaki, Masaaki Browse this author →KAKEN DB | | Tokura, Seiichi Browse this author →KAKEN DB | | Kuboki, Yoshinori Browse this author →KAKEN DB |
| Keywords: | anatase | | chromatography | | collagen | | titanium beads | | 2M urea |
| Issue Date: | May-2021 |
| Publisher: | Oxford University Press |
| Journal Title: | Journal of Biochemistry |
| Volume: | 169 |
| Issue: | 5 |
| Start Page: | 565 |
| End Page: | 573 |
| Publisher DOI: | 10.1093/jb/mvaa146 |
| Abstract: | Titanium is the only metal to which osteoblasts can adhere and on which they can grow and form bone tissue in vivo, resulting in a strong bond between the implant and living bone. This discovery provides the basis for the universal medical application of Ti. However, the biochemical mechanism of bond formation is still unknown. We aimed to elucidate the mechanism of bond formation between collagen, which constitutes the main organic component of bone, and TiO2, of which the entire surface of pure Ti is composed. We analysed the binding between the soluble collagen and TiO2 by chromatography with a column packed with Ti beads of 45 mu m, and we explored the association between collagen fibrils and TiO2 (anatase) powders of 0.2 mu m. We ran the column of chromatography under various elution conditions. We demonstrated that there is a unique binding affinity between Ti and collagen. This binding capacity was not changed even in the presence of the dissociative solvent 2M urea, but it decreased after heat denaturation of collagen, suggesting the contribution of the triple-helical structure. We propose a possible role of periodically occurring polar amino acids and the collagen molecules in the binding with TiO2. |
| Type: | article |
| URI: | http://hdl.handle.net/2115/82494 |
| Appears in Collections: | 環境科学院・地球環境科学研究院 (Graduate School of Environmental Science / Faculty of Environmental Earth Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
|
|
