Premium
Fine‐tuning the π–π Aromatic Interactions in Peptides: Somatostatin Analogues Containing Mesityl Alanine
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 - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201106406
Subject(s) - somatostatin , alanine , chemistry , combinatorial chemistry , peptide , stereochemistry , biochemistry , medicine , amino acid
Going through the motions : Somatostatin analogues having greater conformational rigidity than somatostatin have been prepared by substituting Phe residues in the native sequence with mesityl alanine (Msa; see structure). The analogues show high affinity for SSTR receptors, thus showing that fine‐tuning of noncovalent interactions between amino acid side chains can modulate peptide affinity and selectivity.