Synthesis of N-Glycosylated Soluble Fas Ligand

Alanca Schmid, Claudia Bello, Christian F.W. Becker (Corresponding author)

Publications: Contribution to journalArticlePeer Reviewed

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 languageEnglish
Article numbere202400120
JournalChemistry - A European Journal
Volume30
Issue number24
Early online date16 Feb 2024
DOIs
Publication statusPublished - 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

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