@article{194,
  author = {E. Szolnoki and A. Hetenyi and István Mándity and Ferenc Fülöp and Tamás Martinek},
  title = {Foldameric β-H18/20P mixed helix stabilized by head-to-tail contacts: A way to higher-order structures},
  abstract = {Peptidic foldamers are known to exhibit increased diversity in the periodic secondary-structure space in comparison with their natural counterparts, but their higher-order self-organization has been studied less thoroughly. In theory, large-diameter peptide foldamer helices have the capability of self-recognition through axial helix-helix interactions (e.g., head-to-tail), but this phenomenon has previously been observed in only one instance. In this article we report on the discovery of the largest-diameter β-peptidic mixed helix to date, the H18/20P helix. Its formation is solvent-dependent and its folding occurs cooperatively through head-to-tail self-assembly in solution. These findings suggest that axial helix-helix interactions can serve as a new mode for the formation of tertiary/quaternary structures for peptide foldamers, which also show higher-order structural diversity than natural proteins. © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.},
  year = {2013},
  journal = {European Journal of Organic Chemistry},
  volume = {2016},
  number = {17},
  pages = {3555–3559},
  address = {Guichard, G., Huc, I., (2011) Chem. Commun., 47, p. 5933;},
  issn = {1434-193X},
}