Chemical chaperone
From Wikipedia, the free encyclopedia
Chemical chaperones are small molecules that stabilize the folding of proteins and buffer abnormal protein aggregation seen in proteopathy.[1] These compounds include 4-phenylbutyrate (4-PBA), tauroursodeoxycholic acid (TUDCA) and trehalose.[2]
See also
- Chaperone (protein), proteins that perform the same function
References
- ↑ "Influence of molecular and chemical chaperones on protein folding". Cell Stress Chaperones. PMC 248462.
- ↑ "Chemical Chaperones Reduce Endoplasmic Reticulum Stress and Prevent Mutant HFE Aggregate Formation". Journal of Biological Chemistry. doi:10.1074/jbc.M702672200.
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