Inside Back Cover
Inside Back Cover: Fine-tuning the π–π Aromatic Interactions in Peptides: Somatostatin Analogues Containing Mesityl Alanine (Angew. Chem. Int. Ed. 8/2012)
Article first published online: 5 JAN 2012
DOI: 10.1002/anie.201108928
Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Additional Information
How to Cite
Martín-Gago, P., Gomez-Caminals, M., Ramón, R., Verdaguer, X., Martin-Malpartida, P., Aragón, E., Fernández-Carneado, J., Ponsati, B., López-Ruiz, P., Cortes, M. A., Colás, B., Macias, M. J. and Riera, A. (2012), Inside Back Cover: Fine-tuning the π–π Aromatic Interactions in Peptides: Somatostatin Analogues Containing Mesityl Alanine (Angew. Chem. Int. Ed. 8/2012). Angew. Chem. Int. Ed., 51: 1977. doi: 10.1002/anie.201108928
Publication History
- Issue published online: 14 FEB 2012
- Article first published online: 5 JAN 2012
- Abstract
- Cited By
Keywords:
- conformation analysis;
- NMR spectroscopy;
- noncovalent interactions;
- peptides;
- drug design

The π–π aromatic interactions between amino acids 6, 7, and 11 in the natural hormone somatostatin are crucial for conformational stability. In their Communication on page 1820 ff., M. J. Macias, A. Riera, and co-workers describe that peptidic analogues obtained by replacing each phenylalanine with mesitylalanine are conformationally more rigid than the parent hormone. This strategy has yielded the first 3D structures of 14-amino-acid somatostatin analogues.

1521-3773/asset/2002_left.gif?v=1&s=ac6b0d94a94d7ce7a210002b8096b42feffc0bcf)
1521-3773/asset/2002_right.gif?v=1&s=451042aa3415ae3ad0729984d26dee1866aca82e)
