Mutational analysis of human tumor necrosis factor-alpha
- Authors
- Shin, HC; Cho, KH
- Issue Date
- Jan-2005
- Publisher
- SPRINGER
- Keywords
- cytotoxicity; muteins; receptor binding; structure-function relationship; tumor necrosis factor-alpha
- Citation
- BIOTECHNOLOGY LETTERS, v.27, no.2, pp.107 - 112
- Journal Title
- BIOTECHNOLOGY LETTERS
- Volume
- 27
- Number
- 2
- Start Page
- 107
- End Page
- 112
- URI
- http://scholarworks.bwise.kr/ssu/handle/2018.sw.ssu/19408
- DOI
- 10.1007/s10529-004-6937-y
- ISSN
- 0141-5492
- Abstract
- To understand the structure-function relationship of human tumor necrosis factor-alpha ( TNF-alpha), mutational analysis was carried out on the lower regions ( regions 1-6) of the molecule. The muteins were prepared as a soluble form by using a chaperonin co-expression system and the cytotoxic activities of the purified muteins were evaluated on TNF-sensitive murine. fibrosarcoma L929 cells. Three regions ( regions 1, 2 & 4) were found where mutations significantly influenced the bioactivity. In region 1 ( residues 1-10), the number of deleted residues and the positioning of positive charges are important to achieve a maximum activity and in region 4 ( residues 84-88), introduction of charged residues in one of the positions 86-88 significantly increased the cytotoxic activity. On the other hand, any mutation introduced in region 2 ( residues 37-41) had a deleterious effect. The present study provides a structural basis for the design of highly potent TNF-alpha as a therapeutic agent.
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Collections - College of Natural Sciences > School of Systems and Biomedical Science > 1. Journal Articles
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