Implications of replacing peptide bonds in the COOH-terminal B chain domain of insulin by the psi (CH2-NH) linker.

@article{Nakagawa1993ImplicationsOR,
  title={Implications of replacing peptide bonds in the COOH-terminal B chain domain of insulin by the psi (CH2-NH) linker.},
  author={Satoe H. Nakagawa and Nils Langeland Johansen and Kjeld Kilsgaard Madsen and Thue W. Schwartz and Howard S. Tager},
  journal={International journal of peptide and protein research},
  year={1993},
  volume={42 6},
  pages={578-84}
}
To evaluate more thoroughly the importance of main-chain structure and flexibility in ligand interactions with the insulin receptor, we undertook to synthesize analogues with reduced peptide bonds in the COOH-terminal B chain domain of the hormone (a stable, but adjustable beta-strand region). By use of solid-phase, solution-phase and semisynthetic methods, analogues were prepared in which ArgB22 of des-octapeptide(B23-B30)-insulin was extended by the sequences Gly-Phe-psi (CH2-NH)-Phe-NH2, Gly… CONTINUE READING