AI Article Synopsis
- A new protein conjugation method called GlyConnect-oxime (GC) has been developed as an extension to the existing GlycoDelete (GD) technology, which allows for site-selective attachment of glycans to proteins.
- The GlycoDelete technique creates glycoproteins with specific types of glycans, making it easier to perform site-selective conjugation due to their unique properties.
- The current research explores using multicomponent reactions, like Ugi and Passerini, to enhance this process by allowing multiple groups to be introduced in one step while maintaining a hydrophilic peptide-like linker.
Article Abstract
Recently, the GlyConnect-oxime (GC) protein conjugation strategy was developed to provide a site-selective glycan-based conjugation strategy as an extension to the in-house developed GlycoDelete (GD) technology. GD gives access to glycoproteins with single GlcNAc, LacNAc, or LacNAc-Sia type glycans on their -glycosylation sites. We have previously shown that these glycans provide a unique handle for site-selective conjugation as they provide a short, homogeneous and hydrophilic link to the protein backbone. GC focused on the use of chemical and chemo-enzymatic pathways for conjugation of a single molecule of interest oxime formation or reductive amination. In the current work, we explore multicomponent reactions (MCR), namely Ugi and Passerini reactions, for GlycoDelete glycan directed, site-specific protein conjugation (MC-GC). The use of the Ugi and Passerini multicomponent reactions holds the potential of introducing multiple groups of interest in a single reaction step while creating a hydrophilic peptide-like linker.
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| http://dx.doi.org/10.1039/d1ob02299g | DOI Listing |
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