Apolipoprotein A-I (apoA-I) is a major component of High Density Lipoproteins (HDL) and is comprised of 6 amphipathic α-helices in an N-terminal bundle and a smaller C-terminal region. Studies have suggested that HDL and apoA-I have the ability to neutralize the effects of lipopolysaccharides (LPS), the major cause of sepsis. ApoA-I was acetylated to neutralize the positive charge of the lysine residues prior to determining the effects on LPS binding. The acetylation procedure did not alter the stability of apoA-I though the α-helical content was reduced. Upon analysis by mass spectrometry it was determined that nearly 1000% of the lysine residues were neutralized. Using NativePAGE, Far-UV analysis, 1-anilinonaphthalene-8-sulfonate, and tryptophan fluorescence it was determined that when the positive lysine residues were neutralized, LPS binding was strongly impaired, indicating that lysine residues have a critical role in LPS binding.
|Advisor:||Weers, Paul M. M.|
|Commitee:||McAbee, Douglas D., Narayanaswami, Vasanthy, Weers, Paul M. M.|
|School:||California State University, Long Beach|
|School Location:||United States -- California|
|Source:||MAI 51/04M(E), Masters Abstracts International|
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