@article{BartoloniJinMarcaidaetal.2015,
  author    = {Bartoloni, Marco and Jin, Xian and Marcaida, Maria Jos{\´e} and Banha, Joao and Dibonaventura, Ivan and Bongoni, Swathi and Bartho, Kathrin and Gr{\"a}bner, Olivia and Sefkow, Michael and Darbre, Tamis and Reymond, Jean-Louis},
  title     = {Bridged bicyclic peptides as potential drug scaffolds},
  series = {Chemical Science},
  volume    = {10},
  journal   = {Chemical Science},
  number    = {6},
  publisher = {Royal Society of Chemistry},
  address   = {Cambridge},
  issn      = {2041-6520},
  doi       = {10.1039/C5SC01699A},
  pages     = {5473 -- 5490},
  year      = {2015},
  abstract  = {Double cyclization of short linear peptides obtained by solid phase peptide synthesis was used to prepare bridged bicyclic peptides (BBPs) corresponding to the topology of bridged bicyclic alkanes such as norbornane. Diastereomeric norbornapeptides were investigated by 1H-NMR, X-ray crystallography and CD spectroscopy and found to represent rigid globular scaffolds stabilized by intramolecular backbone hydrogen bonds with scaffold geometries determined by the chirality of amino acid residues and sharing structural features of β-turns and α-helices. Proteome profiling by capture compound mass spectrometry (CCMS) led to the discovery of the norbornapeptide 27c binding selectively to calmodulin as an example of a BBP protein binder. This and other BBPs showed high stability towards proteolytic degradation in serum.},
  language  = {en}
}
@misc{BartoloniJinMarcaidaetal.2015,
  author    = {Bartoloni, Marco and Jin, Xian and Marcaida, Maria Jos{\´e} and Banha, Joao and Dibonaventura, Ivan and Bongoni, Swathi and Bartho, Kathrin and Gr{\"a}bner, Olivia and Sefkow, Michael and Darbre, Tamis and Reymond, Jean-Louis},
  title     = {Bridged bicyclic peptides as potential drug scaffolds},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-81239},
  year      = {2015},
  abstract  = {Double cyclization of short linear peptides obtained by solid phase peptide synthesis was used to prepare bridged bicyclic peptides (BBPs) corresponding to the topology of bridged bicyclic alkanes such as norbornane. Diastereomeric norbornapeptides were investigated by 1H-NMR, X-ray crystallography and CD spectroscopy and found to represent rigid globular scaffolds stabilized by intramolecular backbone hydrogen bonds with scaffold geometries determined by the chirality of amino acid residues and sharing structural features of β-turns and α-helices. Proteome profiling by capture compound mass spectrometry (CCMS) led to the discovery of the norbornapeptide 27c binding selectively to calmodulin as an example of a BBP protein binder. This and other BBPs showed high stability towards proteolytic degradation in serum.},
  language  = {en}
}