What is it about?
Duchenne muscular dystrophy (DMD) is a fatal muscle disease caused by the loss of dystrophin, a protein that protects muscle cells from damage during movement. A related protein, utrophin, is being explored as a possible replacement therapy, but it is unclear whether it functions the same way. This study examines whether utrophin, a protein similar to dystrophin, can mechanically replace dystrophin in muscle cells. Using single molecule force measurements, we directly compared how dystrophin and utrophin respond to physical stress. We found that dystrophin unfolds in a way that helps absorb mechanical stress, while utrophin behaves more like a stiff spring.
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Why is it important?
Our results show that dystrophin and utrophin are not mechanically equivalent, suggesting utrophin may not fully protect muscle cells. This insight is critical for evaluating and improving DMD treatment strategies.
Read the Original
This page is a summary of: Multiple modes of AFM reveal distinct mechanical properties for dystrophin and utrophin not manifest by small fragments, Proceedings of the National Academy of Sciences, January 2026, Proceedings of the National Academy of Sciences,
DOI: 10.1073/pnas.2511722123.
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