@article{FischerLampingGoldetal.2017,
  author    = {Fischer, Sabrina and Lamping, Matthias and Gold, Maike and R{\"o}ttger, Yvonne and Br{\"o}dje, D{\"o}rte and Dodel, Richard and Frantz, Renate and Mraheil, Mobarak Abu and Chakraborty, Trinad and Geyer, Armin},
  title     = {Synthesis of a biological active β-hairpin peptide by addition of two structural motifs},
  series = {Bioorganic \& Medicinal Chemistry},
  volume    = {25},
  journal   = {Bioorganic \& Medicinal Chemistry},
  number    = {2},
  issn      = {0968-0896},
  doi       = {10.1016/j.bmc.2016.11.022},
  pages     = {603 -- 608},
  year      = {2017},
  abstract  = {The idea of privileged scaffolds - that there seem to be more bioactive compounds found around some structures than others - is well established for small drug molecules, but has little significance for standalone peptide secondary structures whose adaptable shapes escape the definition of a 3D motif in the absence of a protein scaffold. Here, we joined two independent biological functions in a single highly restricted peptide to support the hypothesis that the β-hairpin shape is the common basis of two otherwise unrelated biological recognition processes. To achieve this, the hydrophobic cluster HWX4LV from the decapeptide cyclic hairpin model peptide C1-C10 cyclo-CHWEGNKLVC was included in the bicyclic peptide 2. The designed β-hairpin peptide C4-C17, C8-C13 bicyclo-KHQCHWECTZGRCRLVCGRSGS (2, Z = citrulline), serves, on the one hand, as a specific epitope for rheumatoid autoantibodies and, on the other hand, shows a not negligible antibiotic effect against the bacterial strain E. coli AS19.},
  language  = {en}
}