@article{VacogneWeiTaueretal.2018,
  author    = {Vacogne, Charlotte Dominique and Wei, Chunxiang and Tauer, Klaus and Schlaad, Helmut},
  title     = {Self-assembly of alpha-helical polypeptides into microscopic and enantiomorphic spirals},
  series = {Journal of the american chemical society},
  volume    = {140},
  journal   = {Journal of the american chemical society},
  number    = {36},
  publisher = {American Chemical Society},
  address   = {Washington},
  issn      = {0002-7863},
  doi       = {10.1021/jacs.8b06503},
  pages     = {11387 -- 11394},
  year      = {2018},
  abstract  = {Helical structures are ubiquitous in biological materials and often serve a structural purpose. Bioinspired helical materials can be challenging to synthesize and rarely reach the degree of hierarchy of their natural counterparts. Here we report the first example of particles synthesized by direct emulsification of polypeptides found to display spiral morphologies in the dry state. The polypeptides were alpha-helical homo- and copolypeptides of gamma-benzyl glutamate and allylglycine. The chirality of the spirals was controlled by the chirality of the alpha-helices. Notably, right-handed alpha-helical polypeptides (rich in 1, residues) produced clockwise spirals, whereas left-handed alpha-helical polypeptides (rich in D residues) produced the enantiomorphs, i.e., counterclockwise spirals. The disruption of the alpha-helical conformation by the introduction of chiral defects led to less regular spirals and in some cases their suppression. A hypothesis for the transmission of helicity and chirality from a molecular to a higher hierarchical level, involving fibril bundling of coiled alpha-helices, is proposed.},
  language  = {en}
}