Multiple modes of AFM reveal distinct mechanical properties for dystrophin and utrophin not manifest by small fragments.

ABSTRACT: Duchenne muscular dystrophy (DMD) is a lethal muscle disease caused by the absence of the protein dystrophin. Dystrophin is hypothesized to work as a molecular shock absorber that limits myofiber membrane damage when undergoing reversible unfolding upon muscle stretching and contraction. Here, we report the mechanical characterization of single full-length dystrophin (Dys) molecules using two operational modes of atomic force microscopy; constant speed and constant force as well as Monte Carlo simulations. Furthermore, we have compared Dys with large fragments encoding the N-terminus through spectrin repeat 10 (DysN-R10), the C-terminal retinal isoform of dystrophin (Dp260), and full-length utrophin (Utr). Our comprehensive data reveal that Dys, DysN-R10, and Dp260, all show a uniform, bri

SUBMITTER: Hua C 

PROVIDER: S-EPMC12818407 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature