title: Evaluating quinacrine as a potential amyloid imaging compound: studies on hen egg white lysozyme as model system.
abstract: Amyloid plaque is associated with several neuronal and non-neuronal degenerative diseases. More than twenty human proteins can fold abnormally to form pathological deposits like amyloid plaque. Strategies for treating such diseases include therapies designed to decrease protein plaque formation or its complete clearance, but monitoring/clinical trials of these treatments are limited by the lack of effective methods to monitor amyloid deposits in the organs/tissues of living patients. The current study shows binding and staining ability of quinacrine to protein amyloid deposits, using Hen Egg White Lysozyme (HEWL) as model system and characterization of its binding interaction with HEWL, employing several biophysical techniques. Since quinacrine can pass the blood brain barrier, the current report suggests potential application of quinacrine for antemortem diagnostic of amyloid.
authors: Department of Biotechnology, Indian Institute of Technology Guwahati, Guwahati 781039, Assam, India.
authors: Manjeet
authors: M
authors: Kumar
authors: Nandini
authors: N
authors: Sarkar
authors: Vikash Kumar
authors: VK
authors: Dubey
mesh_terms: D058227:Amyloidogenic Proteins / Q000032:analysis*; D000818:Animals; D002645:Chickens; D003287:Contrast Media; D006801:Humans; D018625:Microscopy, Atomic Force; D009113:Muramidase / Q000032:analysis*; D058225:Plaque, Amyloid / Q000175:diagnosis*; D011796:Quinacrine / Q000737:chemistry; D013050:Spectrometry, Fluorescence; D013194:Staining and Labeling
chemical_list: D058227:Amyloidogenic Proteins; D003287:Contrast Media; C421864:hen egg lysozyme; D009113:Muramidase; D011796:Quinacrine