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

页码：1885 / 1890

页数：6

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