Breakthrough in Understanding Protein Quality Control Mechanism

UMass Amherst researchers uncover critical role of Sep15 in protein folding regulation, opening new avenues for drug development.

Sep15, a rare selenoprotein, forms a key complex with UGGT to manage protein folding.
Misfolded proteins can lead to serious diseases like Alzheimer's and cystic fibrosis.
The study utilized AI model AlphaFold2 to predict the interaction between Sep15 and UGGT.
Disrupting Sep15-UGGT binding confirmed its essential role in protein quality control.
Research paves the way for potential new treatments targeting the Sep15/UGGT interface.