Optimal site-specific PEGylation of mutant TNF-alpha improves its antitumor potency.

@article{Yoshioka2004OptimalSP,
  title={Optimal site-specific PEGylation of mutant TNF-alpha improves its antitumor potency.},
  author={Yasuo Yoshioka and Yasuo M Tsutsumi and Shinji Ikemizu and Yoko Yamamoto and Hiroko Shibata and Toshihide Nishibata and Yohei Mukai and Takayuki Okamoto and Madoka Taniai and Maki Sato Kawamura and Y Abe and Shinsaku Nakagawa and Satoshi Nagata and Yuriko Yamagata and Tadanori Mayumi},
  journal={Biochemical and biophysical research communications},
  year={2004},
  volume={315 4},
  pages={808-14}
}
Recently, we created a lysine-deficient mutant tumor necrosis factor-alpha [mTNF-alpha-Lys(-)] with full bioactivity in vitro compared with wild-type TNF-alpha (wTNF-alpha), and site-specific PEGylation of mTNF-alpha-Lys(-) was found to selectively enhance its in vivo antitumor activity. In this study, we attempted to optimize this PEGylation of mTNF-alpha-Lys(-) to further improve its therapeutic potency. mTNF-alpha-Lys(-) was site-specifically modified at its N-terminus with linear… CONTINUE READING