Apolipophorin-III (apoLp-III), from Galleria mellonella, is an exchangeable apolipoprotein composed of five amphipathic α-helices. Studies have revealed the ability of apoLp-III to provide protection against sepsis by neutralizing the toxicity of lipopolysaccharides (LPS). Binding analysis of apoLp-III and LPS was improved by engineering six single tryptophan mutants containing a tryptophan residue in each helix. The secondary structure of the mutant proteins was similar to that of the wild-type protein, but the protein stability of the mutants was decreased. Using fluorescence spectroscopy, the single tryptophan mutants served to monitor the interactions of the α-helices of apoLp-III when binding to LPS. The λ max values indicated that the helices reside in an intermediate polarity in the presence of LPS. The largest changes in the fluorescence intensity were observed for tryptophans in helix 1 and 5. This indicates that helix 1 and 5 are interacting strongly with LPS.
|Advisor:||Weers, Paul M. M.|
|School:||California State University, Long Beach|
|School Location:||United States -- California|
|Source:||MAI 50/03M, Masters Abstracts International|
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