Effect of Redox Pair on Fibrillogenesis of Amyloid Proteins
Date Issued
2006
Date
2006
Author(s)
Chou, Shang-Wei
DOI
zh-TW
Abstract
At least twenty different human proteins can fold abnormally resulting in the formation of amyloid fibrils and accompanying pathologies. These proteins have little sequence homology; however, they are capable of self-assembling into stable fibrils with a characteristic cross β pleated sheet secondary structure. Although amyloid diseases
have been the center of intense research, the role of amyloid protein and
the toxicity mechanisms that mediate its biological responses remain
rather elusive.
The research presented here is aimed at examining the effect of
relative distribution of the redox pair, the concentration ratio between
reduced and oxidized forms of glutathiones ([GSSG]/[GSH]), in buffer
solution on the in vitro fibrillogenesis/aggregation of two model proteins,
lysozyme and β-amyloid. Using various spectroscopic and analytical
methods, our results demonstrated that around 90% of lysozyme fibril
formation was inhibited in the presence of pure GSH at 2 mM while no
anti-aggregating activity was observed with only GSSG at 2 mM.
Moreover, the presence of GSSG did not seem to affect the inhibitory
potency possessed by GSH when lysozyme was incubated with both
GSSG and GSH. Our results also suggested that the inhibitory activity of
GSH was effective when it was added within 6 days after the initiation of
process. Much less inhibitory effect against fibril formation of Aβ was
found in comparison with lysozyme. We believe that the outcome from
this work will enable us, not only to comprehend the mechanism(s) of
amyloid protein self-assembly, but also to aid in designing potential
targets for amyloidosis.
Subjects
溶菌酶
類澱粉蛋白
雙硫鍵
榖胱甘肽
lysozyme
amyloid protein
disulfide bond
glutathione
SDGs
Type
thesis
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