Heparin and related molecules are complex polysaccharides having numerous pharmaceutical applications: as anti-coagulant, anti-thrombotic and anti- lipemic agents in several medical indications. Also, there is growing body of evidence that heparin plays a key role in neovascularization, breast, prostrate and other cancers, Alzheimer's and other neural diseases etc. Enzymes that degrade heparin-like molecules -heparinases are very specific for defined regions of the polysaccharide backbone. As such, heparinases, are essential reagents in studying structural, biochemical, physiological and pathological roles of heparin. Further, heparinases have shown potential for several diagnostic as well as therapeutic applications. Having cloned the heparinase genes from Flavobacterium heparinum during phase I studies, the phase II objective is to: 1) make very pure recombinant heparinases I. II and III commercially available. Recombinant production enormously facilitates contamination-free expression and cost- effective large scale production of heparinases. This also speeds the pending medical and clinical investigation of heparinases in several applications. 2) perform 'protein engineering' on heparinases to create 'designer' enzymes for different applications 3) develop a method to rapidly generate and separate low molecular weight heparins in a highly reproducible and cost-effective manner. 4) carry feasibility studies in the isolation and cloning of mammalian heparinases for therapeutic applications.

Proposed Commercial Applications

Large-scale production of heparinases will make these enzymes commercially available for several diagnostic as well as therapeutic applications. Further, heparinases are extensively used as important tools in Cell and molecular biology research.

Agency
National Institute of Health (NIH)
Institute
National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
Type
Small Business Innovation Research Grants (SBIR) - Phase II (R44)
Project #
5R44DK051207-03
Application #
2634291
Study Section
Special Emphasis Panel (ZRG3-SSS-2 (01))
Program Officer
Badman, David G
Project Start
1995-09-30
Project End
2000-12-31
Budget Start
1998-02-01
Budget End
2000-12-31
Support Year
3
Fiscal Year
1998
Total Cost
Indirect Cost
Name
Matrix Engineering
Department
Type
DUNS #
City
Medford
State
MA
Country
United States
Zip Code
02155