Exploring the Effects of Naturally Occurring Molecules on the Protein Aggregation
Date Issued
2011
Date
2011
Author(s)
Liu, Kuan-Nan
Abstract
Abnormally folded proteins have been associated with at least twenty-seven debilitating and deadly human diseases. These diseases have distinct clinical, pathological, and biochemical characteristics, resulting in amyloid deposits with similar structures, and their corresponding precursor proteins have unrelated functions and share little sequence homology. Moreover, mounting evidence has suggested that the formation of amyloid fibrils is also possible for a variety of non-disease associated proteins. By taking advantage of this generic fibril-forming property, investigations of the amyloid fibrillation using disease-irrelevant proteins can thus aid in our understanding of possible inhibition of amyloid aggregation. The inhibitors that we used in this study include the predominant short-chain phospholipids that are present in the gray matter of the human brain and the polyphenol (e.g.: curcumin) that is widely used in food spicing and coloring. These naturally-occurring small molecules are accessible and easily absorbed by human body as comparison to the other synthesized polymers, peptides, and molecules.
Our results showed that all the short-chain phospholipids (di-C6-PC and di-C7-PC) and polyphenol (curcumin) are able to attenuate and retard the fibril formation of amyloid-forming proteins, such as bovine insulin and hen egg-white lysozyme. Also, we found that the fibrillar species of bovine insulin and hen egg-white lysozyme formed at acidic pH (pH 2.0) and elevated temperature (55
Subjects
protein aggregation
curcumin
di-acyl-GPC
inhibitor
cytotoxicity
SDGs
Type
thesis
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