Title
Synthesis of N‐Glycosylated Soluble Fas Ligand
Author
Claudia Bello
Interdepartmental Research Unit of Peptide and Protein Chemistry and Biology Department of Chemistry “Ugo Schiff”, University of Florence
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.
Keywords
chemical protein synthesisligationglycosylationdiselenide-selenoester ligationFas ligand
Object type
Language
English [eng]
Persistent identifier
Appeared in
Title
Chemistry – A European Journal
Volume
30
Issue
24
ISSN
0947-6539
Issued
2024
Publication
Wiley
Version type
Date issued
2024
Access rights
Rights
Rights statement
© 2024 The Authors
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