Hybrid peptide design. Hydrogen bonded conformations in peptides containing the stereochemically constrained gamma-amino acid residue, gabapentin.

@article{Vasudev2007HybridPD,
  title={Hybrid peptide design. Hydrogen bonded conformations in peptides containing the stereochemically constrained gamma-amino acid residue, gabapentin.},
  author={Prema G. Vasudev and Kuppanna Ananda and Sunanda Chatterjee and S. Aravinda and Narayanaswamy Shamala and Padmanabhan Balaram},
  journal={Journal of the American Chemical Society},
  year={2007},
  volume={129 13},
  pages={4039-48}
}
The crystal structure of 12 peptides containing the conformationally constrained 1-(aminomethyl)cyclohexaneacetic acid, gabapentin (Gpn), are reported. In all the 39 Gpn residues conformationally characterized so far, the torsion angles about the Calpha-Cbeta and Cbeta-Cgamma bonds are restricted to the gauche conformation (+/-60 degrees ). The Gpn residue is constrained to adopt folded conformations resulting in the formation of intramolecularly hydrogen-bonded structures even in short… CONTINUE READING

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