Protein scaffolds are stable structures capable to recognize and bind, in different conditions, small guest molecules. They are proteins with known conformation which can be used and modified for the construction of variants. The goal of this work is the identification of peptide-based artificial receptors or catalysts. To this purpose, we have considered two different protein motifs to generate new scaffolds: a synthetic E/K coiled-coil domain, and one of the binding sites of the natural protein Human serum albumin. In order to generate stable peptide hosts, we developed peptide libraries to be selected for both properties, adopting two different approaches: RANDOM mutagenesis and SITE-DIRECTED mutagenesis.
