Binding of collagen gene products with titanium oxide

Song, Qin; Iku, Shouhei; Sammons, Rachel; Yagami, Kimitoshi; Furusawa, Toshitake; Morimoto, Koichi; Rahaman, Md Shiblur; Kurasaki, Masaaki; Tokura, Seiichi; Kuboki, Yoshinori

Binding of collagen gene products with titanium oxide

Song, Qin; Iku, Shouhei; Sammons, Rachel et al.

Journal of Biochemistry, 2021, 169(5), 565-573

Permalink : https://hdl.handle.net/2115/82494

このアイテムのアクセス数:549件（2026-08-09 05:33 集計）

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https://doi.org/10.1093/jb/mvaa146			19

論文情報

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アクセス権	open access
URI	https://hdl.handle.net/2115/82494
タイトル	Binding of collagen gene products with titanium oxide
著者	Song, Qin ; Iku, Shouhei ; Sammons, Rachel ; Yagami, Kimitoshi ; Furusawa, Toshitake ; Morimoto, Koichi ; Rahaman, Md Shiblur ; Kurasaki, Masaaki ; Tokura, Seiichi ; Kuboki, Yoshinori
著者名 Song, Qin
著者名 Iku, Shouhei
著者名 Sammons, Rachel
e-Rad_Researcher 00210211 著者名 Yagami, Kimitoshi
著者名 Furusawa, Toshitake
e-Rad_Researcher 10319741 著者名 Morimoto, Koichi
著者名 Rahaman, Md Shiblur
e-Rad_Researcher 80161727 著者名 Kurasaki, Masaaki
e-Rad_Researcher 40000806 著者名 Tokura, Seiichi
e-Rad_Researcher 00014001 著者名 Kuboki, Yoshinori
言語	英語
キーワード	anatase
	chromatography
	collagen
	titanium beads
	2M urea
発行日	2021-05
出版者	Oxford University Press
収録物名	Journal of Biochemistry
巻(号)	169(5)
ページ	565-573
抄録	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.
資源タイプ	学術雑誌論文
出版タイプ	Version of Record
PISSN	0021-924X
関連情報 (isIdenticalTo)	出版社版DOI https://doi.org/10.1093/jb/mvaa146