@article{20967,
  abstract     = {A biotinylated helical aromatic oligoamide foldamer equivalent in size to a 24mer peptide was designed without any prejudice other than to display various polar and hydrophobic side chains at its surface. It was synthesized on solid phase, its P- and M-helical conformers were separated by HPLC on a chiral stationary phase, and the solid state structure of a non-biotinylated analogue was elucidated by X-ray crystallography. Pull-down experiments from a yeast cell lysate using the foldamer as a bait followed by proteomic analysis revealed potential protein binding partners. Three of these proteins were recombinantly expressed. Biolayer interferometry showed submicromolar binding demonstrating the potential of a given foldamer to have affinity for certain proteins in the absence of design considerations. Yet, binding selectivity was low in all three cases since both P- and M-conformers bound to the proteins with similar affinities.},
  author       = {Kwon, Sunbum and Morozov, Vasily and Wang, Lingfei and Mandal, Pradeep K and Chaignepain, Stéphane and Douat, Céline and Huc, Ivan},
  issn         = {1477-0539},
  journal      = {Organic & Biomolecular Chemistry},
  number       = {48},
  pages        = {9342--9347},
  publisher    = {Royal Society of Chemistry},
  title        = {{Interrogating the potential of helical aromatic foldamers for protein recognition}},
  doi          = {10.1039/d4ob01436g},
  volume       = {22},
  year         = {2024},
}

@article{21808,
  abstract     = {A convenient approach for the synthesis of foldable redox-active flavin peptide conjugates was established. A model β-hairpin oligopeptide motif was utilized to demonstrate that azidolysine side-chains are readily functionalised with an alkyne-bearing flavine derivative. The folding equilibrium of the peptide backbone as well as the redox behaviour of the flavin moieties remains intact after the conjugation.},
  author       = {Stricker, Friedrich J and Kölsch, Jonas Christopher and Beil, Sebastian B. and Preiß, Sebastian and Waldvogel, Siegfried R. and Opatz, Till and Besenius, Pol},
  issn         = {1477-0539},
  journal      = {Organic & Biomolecular Chemistry},
  number       = {20},
  pages        = {4483--4486},
  publisher    = {Royal Society of Chemistry},
  title        = {{Facile access to foldable redox-active flavin-peptide conjugates}},
  doi          = {10.1039/d1ob00414j},
  volume       = {19},
  year         = {2021},
}