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The 1,3-diyne linker as a rigid 'i,i+7' staple for α-helix stabilization : stereochemistry at work

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Abstract
Short alphahelical peptide sequences were stabilized through Glaser-Hay couplings of propargylated l- and/or d-serine residues at positions i and i+7. NMR analysis confirmed a full stabilization of the helical structure when a d-Ser (i), l-Ser (i+7) combination was applied. In case two l-Ser residues were involved in the cyclization, the helical conformation is disrupted outside the peptide's macrocycle.
Keywords
constrained peptides, Glaser-Hay coupling, helix stabilization, peptide stapling, PROTEIN-PROTEIN INTERACTIONS, SHORT PEPTIDES, INHIBITORS, MODEL, SPECTROSCOPY, SOFTWARE, BINDING, DESIGN, MDM2

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MLA
Verlinden, Steven, et al. “The 1,3-Diyne Linker as a Rigid ‘i,I+7’ Staple for α-Helix Stabilization : Stereochemistry at Work.” JOURNAL OF PEPTIDE SCIENCE, vol. 25, no. 7, 2019, doi:10.1002/psc.3194.
APA
Verlinden, S., Geudens, N., Van holsbeeck, K., Mannes, M., Martins, J., Verniest, G., & Ballet, S. (2019). The 1,3-diyne linker as a rigid “i,i+7” staple for α-helix stabilization : stereochemistry at work. JOURNAL OF PEPTIDE SCIENCE, 25(7). https://doi.org/10.1002/psc.3194
Chicago author-date
Verlinden, Steven, Niels Geudens, Kevin Van holsbeeck, Morgane Mannes, José Martins, Guido Verniest, and Steven Ballet. 2019. “The 1,3-Diyne Linker as a Rigid ‘i,I+7’ Staple for α-Helix Stabilization : Stereochemistry at Work.” JOURNAL OF PEPTIDE SCIENCE 25 (7). https://doi.org/10.1002/psc.3194.
Chicago author-date (all authors)
Verlinden, Steven, Niels Geudens, Kevin Van holsbeeck, Morgane Mannes, José Martins, Guido Verniest, and Steven Ballet. 2019. “The 1,3-Diyne Linker as a Rigid ‘i,I+7’ Staple for α-Helix Stabilization : Stereochemistry at Work.” JOURNAL OF PEPTIDE SCIENCE 25 (7). doi:10.1002/psc.3194.
Vancouver
1.
Verlinden S, Geudens N, Van holsbeeck K, Mannes M, Martins J, Verniest G, et al. The 1,3-diyne linker as a rigid “i,i+7” staple for α-helix stabilization : stereochemistry at work. JOURNAL OF PEPTIDE SCIENCE. 2019;25(7).
IEEE
[1]
S. Verlinden et al., “The 1,3-diyne linker as a rigid ‘i,i+7’ staple for α-helix stabilization : stereochemistry at work,” JOURNAL OF PEPTIDE SCIENCE, vol. 25, no. 7, 2019.
@article{8619890,
  abstract     = {Short alphahelical peptide sequences were stabilized through Glaser-Hay couplings of propargylated l- and/or d-serine residues at positions i and i+7. NMR analysis confirmed a full stabilization of the helical structure when a d-Ser (i), l-Ser (i+7) combination was applied. In case two l-Ser residues were involved in the cyclization, the helical conformation is disrupted outside the peptide's macrocycle.},
  articleno    = {e3194},
  author       = {Verlinden, Steven and Geudens, Niels and Van holsbeeck, Kevin and Mannes, Morgane and Martins, José and Verniest, Guido and Ballet, Steven},
  issn         = {1075-2617},
  journal      = {JOURNAL OF PEPTIDE SCIENCE},
  keywords     = {constrained peptides,Glaser-Hay coupling,helix stabilization,peptide stapling,PROTEIN-PROTEIN INTERACTIONS,SHORT PEPTIDES,INHIBITORS,MODEL,SPECTROSCOPY,SOFTWARE,BINDING,DESIGN,MDM2},
  language     = {eng},
  number       = {7},
  pages        = {9},
  title        = {The 1,3-diyne linker as a rigid 'i,i+7' staple for α-helix stabilization : stereochemistry at work},
  url          = {http://dx.doi.org/10.1002/psc.3194},
  volume       = {25},
  year         = {2019},
}

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