Glycosidase enzymes have emerged as a potential target for anticancer drug development due to the glycosidases’ ability to catalyze the hydrolysis of glycosidic bonds in complex sugars and the vital role the enzymes play in cellular functions. The hydrolysis of polysaccharides can lead to a range of diseases including diabetes, lysosomal disorders, cystic fibrosis, influenza, Alzheimer’s and cancers. Heparanase is an endolytic enzyme that degrades heparan sulfate polysaccharide chains, which are widely distributed in tissues and have important regulatory and structural functions in the extracellular matrix and at the cell surface. Increased levels of heparanase expression have been associated with disease progression, increased tumor growth, increased angiogenesis, metastatic spread, and poor patient prognosis for both hematological and solid tumor malignancies. Considering these findings, the inhibition of heparanase, a type of glycosidase enzyme, has been targeted as a viable cancer therapeutic.
The current technology consists of anti-heparanase compounds for the treatment of cancer. The anti-heparanase compounds are high affinity, synthetic glycopolymers that result in minimal anticoagulant activity. Stereoselective fluorinated forms of these compounds are also provided.
- Avoidance of anti-coagulation
- High affinity
Applications and Opportunities
- Cancer therapy