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Integrin Ligands with α/β‐Hybrid Peptide Structure: Design, Bioactivity, and Conformational Aspects
Author(s) -
Marco Rossella,
Tolomelli Alessandra,
Juaristi Eusebio,
Gentilucci Luca
Publication year - 2016
Publication title -
medicinal research reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.868
H-Index - 130
eISSN - 1098-1128
pISSN - 0198-6325
DOI - 10.1002/med.21383
Subject(s) - integrin , peptide , chemistry , structure–activity relationship , biochemistry , stereochemistry , computational biology , microbiology and biotechnology , biophysics , biology , receptor , in vitro
Integrins are cell surface receptors for proteins of the extracellular matrix and plasma‐borne adhesive proteins. Their involvement in diverse pathologies prompted medicinal chemists to develop small‐molecule antagonists, and very often such molecules are peptidomimetics designed on the basis of the short native ligand‐integrin recognition motifs. This review deals with peptidomimetic integrin ligands composed of α‐ and β‐amino acids. The roles exerted by the β‐amino acid components are discussed in terms of biological activity, bioavailability, and selectivity. Special attention is paid to the synthetic accessibility and efficiency of conformationally constrained heterocyclic scaffolds incorporating α/β‐amino acid span.