| 초록 |
Tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL) is a type-II transmembrane protein of the TNF superfamiliy. It triggers apoptosis through interaction with the death receptors DR4 and DR5. Interestingly, TRAIL can selectively induce apoptosis of a variety of human tumor cells, but does not seem to be cytotoxic to normal cells. PEGylation has an inherent flexibility because it allows pharmacokinetic profiles to be easily altered by changing the size of the PEG substituent. In particular, increasing PEG size increases protein stability but at the risk of interfering with the biological functions of the proteins involved. Therefore, it is an important point of the optimization of PEG molecular size for the maximization of therapeutic efficacy. We examined that PEG (Mw 2, 5, 10 and 20 kDa)-modified TRAIL at its N-terminal amine were prepared. Then, physicochemical properties, biological activity and stability of PEG-TRAIL derivatives were investigated. |
