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Inside Back Cover: Fine‐tuning the π–π Aromatic Interactions in Peptides: Somatostatin Analogues Containing Mesityl Alanine (Angew. Chem. Int. Ed. 8/2012)
Author(s) -
MartínGago Pablo,
GomezCaminals Marc,
Ramón Rosario,
Verdaguer Xavier,
MartinMalpartida Pau,
Aragón Eric,
FernándezCarneado Jimena,
Ponsati Berta,
LópezRuiz Pilar,
Cortes Maria Alicia,
Colás Begoña,
Macias Maria J.,
Riera Antoni
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201108928
Subject(s) - somatostatin , alanine , int , amino acid , phenylalanine , chemistry , amino acid residue , aromatic amino acids , stereochemistry , peptide , biochemistry , peptide sequence , biology , computer science , endocrinology , gene , operating system
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.