Dissertation/Thesis Abstract

Revisiting Lysozyme and Tri-N-acetylglucosamine Interaction: Preparation and Characterization
by Al-Zuhairi, Wafaa, M.S., Southern Illinois University at Edwardsville, 2014, 56; 1564060
Abstract (Summary)

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.

Indexing (document details)
Advisor: Wei, Chin-Chuan
Commitee: Jones, Myron W., O'Brien, Leah C.
School: Southern Illinois University at Edwardsville
Department: Chemistry
School Location: United States -- Illinois
Source: MAI 53/05M(E), Masters Abstracts International
Source Type: DISSERTATION
Subjects: Biogeochemistry
Keywords: Chitin, Fluorescence spectroscopy, Isothermal titration calorimetry, Lifetime measurement, Lysozyme, Tri-N-acetylglucosamine
Publication Number: 1564060
ISBN: 9781321147186
Copyright © 2019 ProQuest LLC. All rights reserved. Terms and Conditions Privacy Policy Cookie Policy
ProQuest