Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/15683
Title: The molecular mechanisms of the interaction between factor C-derived sushi peptides and bacterial endotoxin
Authors: LI PENG
Keywords: septicaemia, endotoxin, Factor C, Sushi peptides, the molecular interaction, LPS neutralizing
Issue Date: 23-Feb-2007
Source: LI PENG (2007-02-23). The molecular mechanisms of the interaction between factor C-derived sushi peptides and bacterial endotoxin. ScholarBank@NUS Repository.
Abstract: Sushi peptides (S1 and S3) were derived from the endotoxin (lipopolysaccharide, LPS) binding domains of Factor C, which is the LPS-sensor protein in the horseshoe crab. However, the molecular mechanisms of interaction between Sushi peptides and LPS remain unknown. This thesis reports the investigation of the structure-activity relationship of the Sushi peptides using a series of biophysical assays, including fluorescence correlation spectroscopy. S1 is functional as a monomer while S3 is only functional in a dimeric form. Both of Sushi peptides display detergent-like properties in disrupting LPS aggregates. Furthermore, the specificity of the binding of Sushi peptides with LPS-like phospholipids (POPG, palmitoyl-oleoyl-phosphatidylglycerol) is conferred by the electrostatic and hydrophobic forces. The unsaturated nature of the lipid tail confers fluidity to the lipid layer and enhances the activity of the peptides. Thus, the hypothetical models of the interaction between the Sushi peptides and LPS were proposed. Conceivably, Sushi peptides could be potential LPS neutralizing drugs.
URI: http://scholarbank.nus.edu.sg/handle/10635/15683
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