Title |
Two variants of recombinant human bone morphogenetic protein-2 (rhBMP-2) with additional protein domains: Synthesis in an Escherichia coli heterologous expression system
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Published in |
Biochemistry, May 2017
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DOI | 10.1134/s0006297917050091 |
Pubmed ID | |
Authors |
A. S. Karyagina, I. S. Boksha, T. M. Grunina, A. V. Demidenko, M. S. Poponova, O. V. Sergienko, A. M. Lyashchuk, Z. M. Galushkina, L. A. Soboleva, E. O. Osidak, M. S. Bartov, A. V. Gromov, V. G. Lunin |
Abstract |
Two variants of recombinant human bone morphogenetic protein-2 (rhBMP-2) with additional N-terminal protein domains were obtained by expression in E. coli. The N-terminal domains were s-tag (15-a.a. oligopeptide from bovine pancreatic ribonuclease A) and lz (leucine zipper dimerization domain from yeast transcription factor GCN4). The s-tag-BMP-2 and lz-BMP-2 were purified by a procedure that excluded a long refolding stage. The resulting dimeric proteins displayed higher solubility compared to rhBMP-2 without additional protein domains. Biological activity of both proteins was demonstrated in vitro by induction of alkaline phosphatase in C2C12 cells, and the activity of s-tag-BMP-2 in vivo was shown in various experimental animal models. |
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