Amyloid Oligomer Conformation in a Group of Natively Folded Proteins
Author Information
Author(s): Yoshiike Yuji, Minai Ryoichi, Matsuo Yo, Chen Yun-Ru, Kimura Tetsuya, Takashima Akihiko
Primary Institution: Laboratory for Alzheimer's Disease, RIKEN Brain Science Institute, Wako-shi, Saitama, Japan
Hypothesis
The study investigates whether natively folded proteins can exhibit amyloid oligomer conformations.
Conclusion
The study suggests that the amyloid oligomer conformation is present in a group of natively folded proteins, which may play a role in preventing β-aggregation.
Supporting Evidence
- The A11 antibody specifically detects the conformation of amyloid oligomers.
- Chaperones like Hsp27, Hsp70, and Hsp90 were shown to suppress β-aggregation of Aβ.
- Heat treatment of Hsp27 abolished its A11 immunoreactivity and anti-β-aggregation activity.
- Transthyretin and α2-macroglobulin also exhibited anti-β-aggregation activity and A11 immunoreactivity.
Takeaway
Some proteins that are normally folded can also look like harmful amyloid structures, which might help them stop other proteins from clumping together.
Methodology
The study used A11 antibody to probe for amyloid oligomer conformations in various proteins and employed mass spectrometry for analysis.
Limitations
The conformational specificity of A11 for each protein needs further analysis, as the cell lysis procedure might have affected protein conformation.
Statistical Information
P-Value
p=0.00046
Statistical Significance
p<0.05
Digital Object Identifier (DOI)
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