Abstract
Controlled cell death is essential for the regulation of the immune system and plays a role in pathogen defense. It is often altered in pathogenic conditions such as cancer, viral infections and autoimmune diseases. The Fas receptor and its corresponding membrane-bound ligand (FasL) are part of the extrinsic apoptosis pathway activated in these cases. A soluble form of FasL (sFasL), produced by ectodomain shedding, displays a diverse but still elusive set of non-apoptotic functions and sometimes even serves as a pro-survival factor. To gather more knowledge about the characteristics of this protein and the impact N-glycosylations may have, access to homogeneous posttranslationally modified variants of sFasL is needed. Therefore, we developed a flexible strategy to obtain such homogeneously N-glycosylated variants of sFasL by applying chemical protein synthesis. This strategy can be flexibly combined with enzymatic methods to introduce more complex, site selective glycosylations.
Original language | English |
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Article number | e202400120 |
Journal | Chemistry - A European Journal |
Volume | 30 |
Issue number | 24 |
Early online date | 16 Feb 2024 |
DOIs | |
Publication status | Published - 25 Apr 2024 |
Austrian Fields of Science 2012
- 104015 Organic chemistry
- 104004 Chemical biology
- 301902 Immunology
Keywords
- chemical protein synthesis
- diselenide-selenoester ligation
- Fas ligand
- glycosylation
- ligation