Recombinant human bone growth factor BMP-2 obtained by synthesis in Escherichia coli. Part 1: from protein purification to experimental efficiency research models

Gromov A.V.; Poponova M.S.; Karyagina A.S.

doi:https://doi.org/10.17116/molgen20203801124

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Abstract:

The review is devoted to purification and efficiency for bone tissue regenerartion of recombinant BMP-2 obtained by synthesis in Escherichia coli cells in the composition with different materials. The methods of protein synthesis in a heterologous gene expression system with subsequent purification and refolding, resulting in the production of an active dimer of the protein, are described. The effectiveness of BMP-2 of prokaryotic origin for the induction of osteogenesis, not inferior to the efficiency of the protein produced in eukaryotic cells, is shown in numerous studies using a variety of carriers and models in laboratory animals. For literature search we used data bases PubMed Central (U.S. National Institutes of Health’s National Library of Medicine (NIH/NLM)), PubMed (NLM National Center for Biotechnology Information (NCBI)) and e-library («Science Electronic Library»).

Keywords:

BMP-2

Escherichia coli

protein isolation and purification

bone tissue regeneration

osteoplastic materials

review

Authors:

Gromov A.V.

Gamaleya National Research Center of Epidemiology and Microbiology, Ministry of Healthcare of the Russian Federation, Moscow, Russia

Poponova M.S.

Gamaleya National Research Center of Epidemiology and Microbiology, Ministry of Healthcare of the Russian Federation, Moscow, Russia

Karyagina A.S.

Gamaleya National Research Center of Epidemiology and Microbiology, Ministry of Healthcare of the Russian Federation;
All-Russia Research Institute of Agricultural Biotechnology, Russia;
Moscow, Russia;
Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, Moscow, Russia

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References:

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