A Novel Serine Protease Target for Prevention of Breast Cancer by a Soy Bean-Derived Inhibitor
Abstract
In year 2 of our studies of the inhibitory interaction between matriptase and HAl1, and between matriptase and BBI, we have built a 3-D structure of the protease domain of matriptase, based on the homology modeling using the X-ray structure of human thrombin as template. This modeled matriptase structure was used in a structure-based screening of inhibitors. Screening from the NCI small compounds database, we have developed bis-benzamidines as potent matriptase inhibitors. We have also found that, in addition to HAl1, a recently discovered natural trypsin inhibitor, SFTI, from sunflower seed, inhibits matriptase. We have found that in non-transformed mammary epithelial cells, the activated matriptase can be stimulated by lipid phosphates; the activated matriptase is then quickly bound to HAl1, and shed into media.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jul 01, 2001
- Accession Number
- ADA395463
Entities
People
- Robert B. Dickson
Organizations
- Georgetown University