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

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‐tun...

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Bibliographic Details
Authors: Martín-Gago, Pablo, Gomez-Caminals, Marc, Ramón, Rosario, Verdaguer i Espaulella, Xavier, Martin-Malpartida, Pau, Aragón Altarriba, Eric, Fernández-Carneado, Jimena, Ponsati, Berta, López-Ruiz, Pilar, Cortes, María Alicia, Colás, Begoña, Macías Hernández, María J., Riera i Escalé, Antoni
Format: article
Status:Versión aceptada para publicación
Publication Date:2012
Country:España
Institution:Universidad de Barcelona
Repository:Dipòsit Digital de la UB
OAI Identifier:oai:diposit.ub.edu:2445/177099
Online Access:https://hdl.handle.net/2445/177099
Access Level:Open access
Keyword:Somatostatina
Pèptids
Somatostatin
Peptides
Description
Summary: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.

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