Hen egg white (HEW) Lysozyme has been used as protein modeling system for investigation of protein binding and refolding, thus serving as an important tool in recent scientific advances. The Lysozyme protein is also used in the food, dairy, poultry, and pharmaceutical industries. Recently, it has been the subject of attention because Lysozyme protein aggregation has been found in amyloid forms, causing systematic amyloidosis. Thus, its interaction with drugs or inhibitors is being constantly explored to seek possible applications in medicine. Among those chemicals, N–triactylglucosamine (NAG 3) has been shown to be a potent inhibitor, which competes with natural carbohydrate ligands. Therefore, NAG3 may be a potential candidate for inhibiting lysozyme amyloid formation. Here, we describe the isolation of NAG3 from natural sources and studies of its interaction with Lysozyme by ITC, steady state and lifetime fluorescence. The characterization of the isolated product showed similar results with an authentic sample in calorimetry and fluorescence. Lifetime measurements indicated one of six Tryptophan (Trp) residues in Lysozyme increases upon NAG3 binding. Alignment of apo- and NAG3-lysozyme suggests Trp62 or Trp63 is responsible for such lifetime enhancement by stacking with NAG3.
|Commitee:||Jones, Myron W., O'Brien, Leah C.|
|School:||Southern Illinois University at Edwardsville|
|School Location:||United States -- Illinois|
|Source:||MAI 53/05M(E), Masters Abstracts International|
|Keywords:||Chitin, Fluorescence spectroscopy, Isothermal titration calorimetry, Lifetime measurement, Lysozyme, Tri-N-acetylglucosamine|
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