Chaperone proteins protect against desmin fragment amyloid aggregation

Cytoskeletal protein desmin, a cardiac and skeletal intermediate filament that is a major protein component in cardiomyocytes, is believed to be a potential regulator of heart disease. Desmin can cleave into fragments which can form amyloid in vivo, leading to cardiomyopathy. Chaperone proteins ⍺B-crystallin and HSP27 serve to refold, sequester, or disaggregate misfolded or aggregating client proteins and are overexpressed in disease states. In our paper, “Chaperone proteins protect against desmin fragment amyloid aggregation”, we characterize desmin fragment amyloid formation with and without chaperone proteins present and show that these chaperones prevent or delay desmin fragment amyloid formation in a concentration-dependent manner. We also showed that desmin fragment can interact with different domains of these chaperones. Uploaded here are the raw data and MATLAB analysis codes that support the conclusions of our manuscript.