Abstract
Tumor necrosis factor (TNF)-related, apoptosis-inducing ligand (Apo2L/TRAIL) has a unique homotrimeric structure, and its conformational stability is essential for its apoptotic activity. The conformational stability of a modified version of TRAIL(114-281) with two additional domains of histidine tag and isoleucine zipper [His-ILZ-TRAIL(114-281)] was evaluated in various pH environments according to three different biological or physicochemical considerations: cytotoxicity, antibody-binding affinity, and tertiary structure. The biological properties of His-ILZ-TRAIL(114-281) were the most stably maintained at pH 6.0. The physicochemical analyses (circular dichroism and fluorescence spectroscopy) demonstrate that its bioactivity loss by pH challenge was originated from its structural collapse as a homotrimer.
| Original language | English |
|---|---|
| Pages (from-to) | 713-721 |
| Number of pages | 9 |
| Journal | Biotechnology Letters |
| Volume | 29 |
| Issue number | 5 |
| DOIs | |
| State | Published - May 2007 |
UN SDGs
This output contributes to the following UN Sustainable Development Goals (SDGs)
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SDG 3 Good Health and Well-being
Keywords
- Apoptosis
- Conformational
- Homotrimer
- Stability
- TRAIL
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