Progress Report on Contract N00014-94-C-0021 (Massachusetts General Hospital, Boston).
Abstract
This specific aim consists of identifying the LPS binding site of LPS binding protein (LBP). We have completed this goal aim as outlined in our proposal by generating overlapping synthetic peptides and testing for the ability to bind LPS in a slot blot capture system. Fine mapping using this technique suggests that amino acids 86 to 102 are important in the binding. A longer peptide (hLBP76-102) has slightly better binding affinity on a molar basis, perhaps due to stability or secondary and tertiary structure. We initially selected the LBP peptides as perhaps the best candidate for peptide-IgG conjugates because we predicted that the binding affinities would be high and also especially because this is the only LPS binding protein naturally found in the bloodstream. In our hands, most LPS binding peptides that have been described bind with much lower affinity in blood. Since the native holoprotein of LBP mediates and increases LPS-induced cytokine production by greatly facilitating the interaction of LPS with the CDl4 receptor on monocytes
Document Details
- Document Type
- Technical Report
- Publication Date
- Jun 21, 1994
- Accession Number
- ADA299346
Entities
People
- H. S. Warren
Organizations
- Massachusetts General Hospital