Investigating of Amyloid Fibril Formation of Lysozyme and Inhibitors
Date Issued
2005
Date
2005
Author(s)
Chen, Po-Han
DOI
zh-TW
Abstract
More than sixteen different human proteins can fold abnormally resulting in the formation of amyloid fibrils and accompanying pathologies. These proteins have little sequence homology; however, they can polymerize into stable fibrils with a characteristic cross β-sheet structure. Although amyloid diseases have been the center of intense research, the role of amyloid proteins and the associated cytotoxicity mechanisms that mediate biological responses remain largely unknown.
This research, with hen egg white lysozymes utilized as a model system, was set out to study the mechanism(s) of aggregation/fibril formation. First part of the research not only sought out the condition(s) of forming amyloid fibrils but also investigated the relationship between aggregation/fibril formation and environmental factors such as ambient temperature and solvent conditions. Secondly, this work was aimed at examining the inhibitory action of two potential compounds, namely melatonin and benzoquinone, against the aggregation/fibril formation of lysozyme. It was demonstrated that the fibrillar form of hen egg while lysoyzme was able to be produced under the acidic condition (pH 2.0). In addition, the elevated rate of amyloid fibril formation was observed upon salt addition. Our study then showed that benzoquinone exhibited a better anti-aggregating action than melatonin. Finally, in regards to the temperature effect, the lysozymes formed fibrils faster at 70°C in comparison with 37°C and 50°C. We believe that the outcome from this work may contribute to a better understanding of how amyloid proteins polymerize and further facilitate the development of possible strategies to prevent lysozyme or other amyloid protein-associated diseases.
Subjects
溶菌酶
類澱粉纖維
抑制劑
聚集
lysozyme
amyloid fibril
inhibitor
aggregation
SDGs
Type
thesis
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