Two variants of recombinant human bone morphogenetic protein-2 (rhBMP-2) with additional protein domains: Synthesis in an Escherichia coli heterologous expression system
- Resource Type
- Original Paper
- Authors
- Karyagina, A. S.; Boksha, I. S.; Grunina, T. M.; Demidenko, A. V.; Poponova, M. S.; Sergienko, O. V.; Lyashchuk, A. M.; Galushkina, Z. M.; Soboleva, L. A.; Osidak, E. O.; Bartov, M. S.; Gromov, A. V.; Lunin, V. G.
- Source
- Biochemistry (Moscow). May 2017 82(5):613-624
- Subject
- recombinant bone morphogenetic protein-2
heterologous expression
Escherichia coli
- Language
- English
- ISSN
- 0006-2979
1608-3040
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.