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...

Descripción completa

Detalles Bibliográficos
Autores: 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
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2012
País:España
Institución:Universidad de Barcelona
Repositorio:Dipòsit Digital de la UB
OAI Identifier:oai:diposit.ub.edu:2445/177099
Acceso en línea:https://hdl.handle.net/2445/177099
Access Level:acceso abierto
Palabra clave:Somatostatina
Pèptids
Somatostatin
Peptides
Descripción
Sumario: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.

Similares en LA Referencia