Lectenz® Technologies

Lectenz® is able to detect important glycan modifications independent of the sialic acid linkage (e.g.: α2,3 or α2,6 or α2,8), and shows no measurable affinity for related non-sialylated glycans. Such a reagent currently does not exist and would greatly assist in the development and detection of glycan-based disease markers, by enabling affinity enrichment of a sample in the glycopeptides or glycoproteins of interest.

Lectenz® innovate in two distinct ways:

  • The development of glycomics affinity reagents (Lectenz®) from engineered carbohydrate-processing enzymes will create a new class of glycomics reagents, with defined specificities and tunable properties.
  • Employing computational simulations to provide binding energy estimates, which are being used to focus the design of the biocombinatorial libraries and enhancing the efficiency of the bio-panning process

Key Innovations

The key innovations of Lectenz® reagents over existing glycomics reagents are:

Tunable affinities and binding kinetics (essential for applications in an affinity matrix)

Pre-defined, and potentially tunable, specificities – depending on the ligand employed in the directed

Evolution strategy and on the location of the mutagenesis sites

A platform technology that could be applied to a vast number of carbohydrate-processing enzymes

Including glycosyl hydrolases, transferases, lyases, esterases, etc...

What Makes Us Different

Advantage of our engineered Lectenz®:

  • Unlike antibodies, Lectenz® is specific to a carbohydrate sequence and can recognize a broad range of glycans.
  • Lectenz® is derived from enyzmes with a specific substrate specificity, low toxicity and may be able to produce monomeric proteins