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A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis
Published on: May 22, 2018
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Hydrogen sulfide inhibits amyloid formation.
Manuel F Rosario-Alomar1, Tatiana Quiñones-Ruiz, Dmitry Kurouski
1Department of Chemistry and ‡Department of Biology, University of Puerto Rico at Mayagüez , Mayagüez, Puerto Rico 00693.
The Journal of Physical Chemistry. B
|December 30, 2014
Summary
Hydrogen sulfide (H2S) prevents amyloid fibril formation by creating trisulfide bonds, which destabilize proteins. This results in non-toxic, unordered aggregates, offering a new avenue for neurodegenerative disease research.
Area of Science:
- Biochemistry
- Neuroscience
- Structural Biology
Background:
- Amyloid fibrils are linked to neurodegenerative diseases like Alzheimer's.
- Reduced hydrogen sulfide (H2S) levels are observed in Alzheimer's disease brains.
Purpose of the Study:
- To investigate the in vitro effect of H2S on amyloid formation using hen egg white lysozyme (HEWL).
- To understand the molecular mechanism of H2S in preventing protein fibrillation.
Main Methods:
- Deep UV resonance Raman (DUVRR) spectroscopy
- Thioflavin T (ThT) fluorescence assays
- Nonresonance Raman spectroscopy
- TCEP reduction and LC-MS analysis
- Intrinsic tryptophan fluorescence
Main Results:
- H2S completely inhibited the formation of β-sheet and amyloid fibrils.
- H2S induced disulfide bond rearrangements, forming trisulfide (RSSSR) groups.
- Trisulfide bond formation led to HEWL denaturation and prevented fibrillation.
- Non-toxic, unordered protein aggregates were formed in the presence of H2S.
Conclusions:
- H2S prevents HEWL fibrillation by forming trisulfide bridges, destabilizing the protein structure.
- This mechanism offers potential therapeutic insights for amyloid-related neurodegenerative diseases.
- The resulting unordered aggregates are non-cytotoxic, unlike amyloid fibrils.
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