Mapping receptor–ligand interactions with synthetic peptide arrays: Exploring the structure and function of membrane receptors

Development of synthetic peptide array technology started in the early 1990s. The technique originally developed by Ronald Frank has become a powerful tool for high throughput approaches in biology and chemistry mapping protein interaction sites. In this review we focus on peptide arrays applied to investigate receptor–ligand interactions, such as peroxisomal membrane receptor proteins, the maltose importer machinery and receptor proteins recognizing short linear motifs of their partners. We present several systematic sets of peptide arrays useful for mapping protein–protein- or receptor–ligand binding sites. Besides a more technical description of the peptide array preparation we discuss in detail the reliability and improvement of mapping protein–protein interactions by synthetic peptide arrays. At least proteomic approaches for mapping protein–protein interactions by peptide arrays are shown especially for the case of protein interaction domains.