Forms of inherited muscular dystrophy such as Duchenne muscular dystrophy (DMD) and Becker muscular dystrophy (BMD) result from mutations targeting the dystrophin gene. These disorders are X-linked, progressive, and cause the gradual weakening of the muscles leading to respiratory failure and ultimately reduces the patient’s lifespan.

In DMD, mutations lead to the production of premature stop codons and hence the truncated dystrophin protein product is vulnerable to nonsense mediated decay and degradation. Therefore, dystrophin production in muscle cells is reduced. On the other hand, nonsense mutations which also contribute to DMD, cause exon skipping in BMD and result in an internally truncated protein product which are partially functional. The symptoms of BMD are later onset compared with DMD which develop in patients between 2 to 7 years.

Treatments of dystrophin disorders are in clinical trials including antisense oligonucleotide exon skipping and gene therapy. However, the efficacies of these treatments are not easily quantified. Currently levels of muscular dystrophin are quantified by western blot which can be unreliable. The peptide provided here, aligning residues dystrophin (50-61), has been used to try and create a quantifiable method that is reproducible. The method used was not successful, but dystrophin (50-61) remains a useful tool to create a potential quantification method for diagnosis and progress of dystrophin disorders as it was effectively detected by mass spectrometry and Western blot. Within our catalogue we also have other peptides tested for dystrophin quantification available plus the full-length dystrophin protein.