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Large molecule bioconjugation

Bioconjugates made simpler

Benefits of our technology

Facilitates a controlled site-specific conjugation

Straightforward application leading to a cost-effective, high yielding conjugation

Improved stability in comparison to maleimide conjugation

Discovered, validated and patented at ETH Zurich

Thiol CF LINK Bioconjugation

Proteins containing solvent accessible free cysteine residues undergo a controlled, site-specific thiol bioconjugation with Togni-CF2F2R reagents without interference of other nucleophilic groups such as lysines. The S-bound conjugates are formed irreversibly and due to a unique ligation chemistry, they cannot undergo thiol exchange which is observed for conventional Michael acceptors, such as maleimides.

Advantages of our technology

Facilitates a controlled site-specific conjugation

Improved stability in comparison to maleimide conjugation

Tryptophan CF LINK Bioconjugation

Second generation of Togni reagents bearing the RCF2CF2 residues are very easily reduced by sodium ascorbate to generate highly reactive RCF2CF2• fluoroalkyl radicals. When generated in the presence of a protein that contains a solvent accessible tryptophan residue, the protein undergoes a highly site-selective tryptophan bioconjugation even in the presence of other aromatic amino acids.

This technology can be used to introduce a small, β-substituted fluoroalkyl group onto a solvent accessible tryptophan residue of a protein. Depending on the nature of the attached β-substituted fluoroalkyl, various protein modifications can be realized:

  • attachment of toxic/radioactive payloads via click chemistry
  • attachment of fluorescent dyes
  • attachment of stabilizing groups
  • attachment of other small molecules
  • protein immobilisation via click chemistry

 

 

Advantages of our technology

Unique tryptophan-selective bioconjugation

Complementary bioconjugation technology

Transition-metal free bioconjugation

CF LINK surface mapping of proteins

Togni reagents, which belong to the class of hypervalent iodine reagents, are extremely quickly (seconds) reduced by sodium ascorbate to generate highly reactive fluoroalkyl radicals. These in-situ generated fluoroalkyl radicals quickly react with the aromatic, solvent exposed amino acids present in the protein backbone, causing their rapid fluoroalkylation.  Finally, proteolytic digestion and MS-based proteomics reveal which aromatic amino acids are solvent exposed (and thus undergoing fluoroalkylation) and which are solvent inaccessible (and thus immune to fluoroalkylation), either as a consequence of the protein's native structure or due to a binding of a substrate.

This technology can be used to map a protein surface, map the epitope, characterize proteins, probe protein-protein interactions, etc.

Advantages of our technology

Ultrafast surface mapping of aromatic amino acids

Novel, cost effective protein characterisation method

Study of protein-protein interactions

Epitope mapping technology