N-terminal acetylation speeds amyloid formation by SOD1 in a laboratory study
Original source
N-terminal acetylation of superoxide dismutase 1 accelerates amyloid formation without general destabilization of the apo state. (opens in a new tab)Compass summarised this from the study's abstract.
Study details
- Studied in
- Human
Related topics
A study found that adding an N-terminal acetylation modification to the SOD1 protein greatly increased the rate at which it formed amyloid fibrils. The modification did not affect the structure or thermal stability of SOD1 in its unbound state. It shortened the early nucleation phase and increased fibril growth by more than tenfold.
Why this matters
The findings identify a protein modification that may influence how SOD1 misfolds and assembles into fibrils, processes relevant to amyotrophic lateral sclerosis (ALS). This was a laboratory study of protein behaviour and does not show that the modification causes ALS or change treatment for people living with the disease.
Limitations and context
The source is one peer-reviewed primary research article about experiments on purified protein. The reported effects on SOD1 aggregation do not establish what happens in people with ALS, whether the modification drives disease, or whether targeting it would provide a treatment benefit.