APIS Amino acids-Peptidomimetics-peptides-protein InteractionS
M.Luisa Gelmi, Francesca Clerici, Concetta La Rosa, Alessancdro Contini, Emanuela Erba, Sara Pellegrino, Andrea Bonetti, Irene Maffucci, Alessandro Ruffoni.
UNNATURAL AMINO ACIDS
Unusual amino acids provide defined 3D-structural platforms, giving access to complex molecular architecture and finding applications in different fields. A small library of constrained amino acids is available in our lab. We utilize asymmetric synthesis and biocatalysis for the preparation of different classes of unnatural amino acids.
Restricting the local mobility of an oligopeptide is an important goal for the obtainment of bioactive peptidomimetics.
The insertion of unusual amino acids and of covalently constrained scaffolds decreases the available conformational space allowing the modulation of the molecular flexibility.
New architectures using our scaffolds are designed and synthesized.
Stepwise microwave assisted solid phase synthesis is an efficient technique especially for the preparation of difficult and long peptide sequences. By applying MW-SPPS protocols, we prepare small protein domains (e. g. Maf leucine zipper transcription factors) and peptide libraries
Protein interactions are essential to different biological events and their modulation is an effective way to study the mechanisms governing cellular activity, leading to the discovery of new biomolecular tools. Synergic activity of molecular modeling, synthesis and characterization allows us to develop new molecules targeted on different proteins (e.g. Rac, Maf, Tubulin).