title: Formation of α-helix-based twisted ribbon-like fibrils from ionic-complementary peptides.
abstract: Ionic-complementary peptides (ICPs) are well known for their strong propensity to form amyloid-like β-sheet fibrils. Here, we present the first example that α-helical based ICPs can self-assemble into a highly ordered fibrillar structure. Intriguingly, the individual α-helices in such fibrils are arranged shoulder-to-shoulder, making them distinct from conventional coiled-coil-based fibrils.
authors: National Laboratory of Solid State Microstructure and Department of Physics, Nanjing University, Nanjing 210093, China.
authors: Dawei
authors: D
authors: Zou
authors: Yi
authors: Y
authors: Cao
authors: Meng
authors: M
authors: Qin
authors: Weimin
authors: W
authors: Dai
authors: Wei
authors: W
authors: Wang