4.0 Article

Expression and properties of human TNF peptide fragments

Journal

RUSSIAN JOURNAL OF BIOORGANIC CHEMISTRY
Volume 36, Issue 3, Pages 301-309

Publisher

MAIK NAUKA/INTERPERIODICA/SPRINGER
DOI: 10.1134/S1068162010030040

Keywords

tumor necrosis factor; E. coli expression; informational structure; peptides; cytotoxicity

Funding

  1. Russian Academy of Sciences [SS-5207.2010.4]

Ask authors/readers for more resources

The tumor necrosis factor (TNF) is a proinflammatory cytokine that plays a pivotal role in the regulation of the human immune system. Studies of the TNF functional topography are a challenging task in bioengineering. We have produced genes encoding the peptides D1 (3-30), D2 (31-85), D3 (86-114), and D4 (115-157), which correspond to isolated fragments of the informational structure of TNF. These genes were expressed in E. coli cells at a high level in a soluble form. We have shown that hybrid proteins SD2 and SD4 tend to form high-molecular aggregates, which can be destroyed by urea treatment. Purified peptides D1, D3, and D4 possess a similar secondary structure with dominating beta-structural elements. The analysis of the biological activity of these peptides has shown that they do not exhibit cytotoxic properties on L929 murine fibroblasts. The simultaneous addition of D1 with full-length TNF results in the concentration dependent suppression of TNF activity.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.0
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available