Recombinant hBMP4 incorporated with non-canonical amino acid for binding to hydroxyapatite

被引：17
|
作者：
Sakuragi, Makoto [1 ]
Kitajima, Takashi [1 ]
Nagamune, Teruyuki [2 ]
Ito, Yoshihiro [1 ]
机构：
[1] RIKEN, Adv Sci Inst, Nano Med Engn Lab, Wako, Saitama 3510198, Japan
[2] Univ Tokyo, Sch Engn, Dept Bioengn, Bunkyo Ku, Tokyo 1138656, Japan
来源：
BIOTECHNOLOGY LETTERS | 2011年 / 33卷 / 09期
关键词：
BMP protein; Hydroxyapatite; Non-canonical amino acid; Phosphorylated serine; Protein engineering; Sortase A; Statherin; STATHERIN; SORTASE; BMP-2; DIFFERENTIATION; CONFORMATION; OSTEOPONTIN; PEPTIDES; PROTEINS; SEQUENCE; SURFACES;
D O I：
10.1007/s10529-011-0637-1
中图分类号：
Q81 [生物工程学（生物技术）]; Q93 [微生物学];
学科分类号：
071005 ; 0836 ; 090102 ; 100705 ;
摘要：
A novel growth factor containing non-canonical amino acids was designed and synthesized to enhance the binding to hydroxyapatite (HA). The designed protein was human bone morphogenetic protein 4 (hBMP4) incorporating diphosporylated serines (pSpS) that was found in salivary protein statherin and was reported to be responsible for binding to HA. Recombinant hBMP4 and a short peptide sequences containing pSpS were ligated by enzymatice reaction of sortase A, which exchanges the terminal amino acids of two polypeptides. Resulting hBMP4 containing pSpS (hBMP4-pSpS) bound HA more efficiently than hBMP-4 tagged with canonical serines (hBMP4-SS). The HA-bound hBMP-4-pSpS exhibited osteogenesis inducing activity to multipotential mesenchyme cells (C3H10T1/2) as evidenced by increased expression of osteogenic markers, which was not seen by hBMP4-SS. This novel protein with non-canonical serines will be applicable to bone regeneration materials in combination with HA.
引用
收藏
页码：1885 / 1890
页数：6
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