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Protein & Peptide Letters


ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Evaluating Quinacrine as a Potential Amyloid Imaging Compound: Studies on Hen Egg White Lysozyme as Model System

Author(s): Manjeet Kumar, Nandini Sarkar and Vikash Kumar Dubey

Volume 19, Issue 8, 2012

Page: [826 - 831] Pages: 6

DOI: 10.2174/092986612801619598

Price: $65


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.

Keywords: Amyloid plaque, fluorescence quenching, FTIR, hen egg white lysozyme, imaging, quinacrine, fibrillar protein, Alzheimer’s disease, Parkinson’s Disease, Type II Diabetes Mellitus

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