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.
Keywords: Amyloid plaque, fluorescence quenching, FTIR, hen egg white lysozyme, imaging, quinacrine, fibrillar protein, Alzheimer’s disease, Parkinson’s Disease, Type II Diabetes Mellitus
Protein & Peptide Letters
Title:Evaluating Quinacrine as a Potential Amyloid Imaging Compound: Studies on Hen Egg White Lysozyme as Model System
Volume: 19 Issue: 8
Author(s): Manjeet Kumar, Nandini Sarkar and Vikash Kumar Dubey
Affiliation:
Keywords: Amyloid plaque, fluorescence quenching, FTIR, hen egg white lysozyme, imaging, quinacrine, fibrillar protein, Alzheimer’s disease, Parkinson’s Disease, Type II Diabetes Mellitus
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.
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Cite this article as:
Kumar Manjeet, Sarkar Nandini and Kumar Dubey Vikash, Evaluating Quinacrine as a Potential Amyloid Imaging Compound: Studies on Hen Egg White Lysozyme as Model System, Protein & Peptide Letters 2012; 19 (8) . https://dx.doi.org/10.2174/092986612801619598
DOI https://dx.doi.org/10.2174/092986612801619598 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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