# name
Fine-tuning the [Pi]-[Pi]. Aromatic interactions in peptides: somatostatin analogues containing mesityl alanine

# metadata.dc.description.abstract[].value
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.

# metadata.dc.relation.ispartof[].value
Angewandte Chemie-International Edition, 2012, vol. 51, num. 8, p. 1820-1825

# metadata.dc.source[].value
Articles publicats en revistes (Química Inorgànica i Orgànica)

# metadata.dc.title[].value
Fine-tuning the [Pi]-[Pi]. Aromatic interactions in peptides: somatostatin analogues containing mesityl alanine