BDTI found that there was an unmet need in the field for specific, efficient endotoxin removal. Most chromatography ligands are non-specific and result in incomplete removal and/or significant loss of product. The non-specificity also causes these products to be sensitive to buffer conditions. To address this, BDTI partnered with the National University of Singapore (NUS). Scientists at NUS dissected the enzymatic cascade of the Limulus amebocyte lysate (LAL) assay and identified the molecular site where endotoxin binds to Factor C, the initiating enzyme. A peptide consisting of this endotoxin-binding Sushi domain can be made chemically. The peptide can be coupled to a support for efficient endotoxin removal over a wide range of buffer conditions with minimal product loss.
BDTI is also concerned with accurate endotoxin detection. One significant issue associated with accurate endotoxin detection is endotoxin masking. Masking occurs when the product being tested tightly binds endotoxin and prevents it from being recognized by the assay. This can result in potentially dangerous false negatives. Assays affected by endotoxin masking include classical LAL, recombinant Factor C and endotoxin-specific ELISA. BDTI has developed patented technologies which enzymatically remove masking prior to testing, resulting in accurate results and control reactions.
Recently, BDTI has begun to develop a bioassay system to monitor disease in conditions that have inflammation due to endotoxin exposure as a result of bacterial translocation from the gut. This includes a published study in inflammatory bowel disease (Champion, et al.) and an ongoing study in HIV infection.