Fusion to an albumin-binding domain with a high affinity for albumin extends the circulatory half-life and enhances the in vivo antitumor effects of human TRAIL.

@article{Li2016FusionTA,
  title={Fusion to an albumin-binding domain with a high affinity for albumin extends the circulatory half-life and enhances the in vivo antitumor effects of human TRAIL.},
  author={Rui Li and Hao Yang and Dianlong Jia and Qianxue Nie and Huawei Cai and Qing Fan and Lin Wan and Lin Li and Xiaofeng Lu},
  journal={Journal of controlled release : official journal of the Controlled Release Society},
  year={2016},
  volume={228},
  pages={96-106}
}
Clinical applications of recombinant human tumor necrosis factor-related apoptosis-inducing ligand (hTRAIL) have been limited by their poor pharmacokinetics. Using endogenous albumin as a carrier is an attractive approach for circulatory half-life extension. Here, we produced ABD-hTRAIL and hTRAIL-ABD by fusing the albumin-binding domain (ABD) from protein G to the N- or C-terminus of hTRAIL. We found that ABD-hTRAIL bound human serum albumin (HSA) with a high affinity (0.4 ± 0.18 nM) and… CONTINUE READING