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Accepted version

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2012-02

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Please use this identifier to cite or link to this item: https://hdl.handle.net/2445/177099

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

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https://doi.org/10.1002/anie.201106406

Abstract

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.

Subject

Somatostatina, Pèptids

Subject (English)

Somatostatin, Peptides

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Articles publicats en revistes (Química Inorgànica i Orgànica)

Citation

MARTÍN-GAGO, Pablo, et al. Fine-tuning the [Pi]-[Pi]. Aromatic interactions in peptides: somatostatin analogues containing mesityl alanine. Angewandte Chemie-International Edition. 2012. Vol. 51, num. 8, pags. 1820-1825. ISSN 1433-7851. [consulted: 19 of August of 2026]. Available at: https://hdl.handle.net/2445/177099

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