This research was supported by a grant from the Council of Scientific and Industrial Research (CSIR) and Program Support in the area of Molecular Diversity and Design, Department of Biotechnology, India. We thank Dr. K. Nagarajan of Hikal R&D Centre, Bangalore (India), for the sample of gabapentin. P.G.V. and K.A. thank the CSIR for a senior research fellowship and research associateship, respectively. X-ray diffraction data were collected on the CCD facility funded under the IRHPA program of the Department of Science and Technology, India.
C9 Helices and Ribbons in γ-Peptides: Crystal Structures of Gabapentin Oligomers†
Article first published online: 8 JUL 2005
Copyright © 2005 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 44, Issue 31, pages 4972–4975, August 5, 2005
How to Cite
Vasudev, P. G., Shamala, N., Ananda, K. and Balaram, P. (2005), C9 Helices and Ribbons in γ-Peptides: Crystal Structures of Gabapentin Oligomers. Angew. Chem. Int. Ed., 44: 4972–4975. doi: 10.1002/anie.200501055
- Issue published online: 29 JUL 2005
- Article first published online: 8 JUL 2005
- Manuscript Received: 23 MAR 2005
- helical structures;
- hydrogen bonds;
- peptide conformation;
- ribbon structures
Nine is the number: Novel C9-hydrogen-bonded structures (in which the hydrogen bonds enclose a ring of nine atoms) are observed in protected di- and tetrapeptides formed by the γ-amino acid residue gabapentin. The structures reveal new families of C9 helices and ribbons (see structure) in γ-polypeptides.