In the current issue of Nature Materials, polymer scientists Greg Grason, Douglas Hall and Isaac Bruss at the University of Massachusetts Amherst, with Justin Barone at Virginia Tech, identify for the first time the factors that govern the final morphology of self-assembling chiral filament bundles. They also report experimental results supporting their new model.
At the molecular level, Grason explains, chiral filament bundles are many-stranded, self-twisting, yarn-like structures. One example are amyloid fibers, assemblies of misfolded proteins linked to diseases like Alzheimer’s and Parkinson’s. Many other proteins take this shape, including collagen, the most abundant protein in the body, and sickle-hemoglobin proteins found in sickle-cell anemia. But how they attain their final size and shape has not been well understood.
Read full story at: UMass Amherst News Office