Disulfide Bonds Reduce the Toxicity of the Amyloid Fibrils Formed by an Extracellular Protein
2011
Disulfide Bonds and Amyloid Fibrils
publication
Evidence: high
Author Information
Author(s): Mossuto Maria F, Bolognesi Benedetta, Guixer Bernat, Dhulesia Anne, Agostini Federico, Kumita Janet R, Tartaglia Gian G, Dumoulin Mireille, Dobson Christopher M, Salvatella Xavier
Primary Institution: Institute for Research in Biomedicine (IRB Barcelona)
Hypothesis
Do disulfide bonds influence the formation and toxicity of amyloid fibrils?
Conclusion
Disulfide bonds reduce the toxicity of amyloid fibrils by stabilizing their structure.
Supporting Evidence
- Disulfide bonds stabilize folded proteins and influence amyloid fibril formation.
- Fibrils formed by reduced lysozyme are more toxic than those formed by wild-type lysozyme.
- Disulfide bonds are prevalent in extracellular proteins to minimize toxic aggregation.
Takeaway
Disulfide bonds help proteins stay in their proper shape, which makes them less likely to form harmful clumps.
Methodology
The study examined the formation of amyloid fibrils by human lysozyme with and without disulfide bonds using various biophysical techniques.
Statistical Information
P-Value
p<0.0001
Statistical Significance
p<0.0001
Digital Object Identifier (DOI)
Want to read the original?
Access the complete publication on the publisher's website