"Peptides are among the most versatile natural products that nature provides to cater for a broad set of biotechnological applications ranging from antibiotics to personal hygiene. Their diversity comes from a broad variety of posttranslational modifications that is used to provide additional functionality beyond to what is possible with the classic proteinogenic set of 20 amino acids. In SYNPEPTIDE, we want to recruit such additional functionality for rational molecular design purposes in order to facilitate the design and the production of synthetic peptides.
To this end, we intend to standardize the integration of chemical diversity in peptide design and production by the following activities: [i] translational integration of chemically suitable non-canonical amino acids for posttranslational in vivo and in vitro modification; [ii] systematic recruitment of selected highly relevant posttranslational modifications from natural peptide synthesis routes into the design process. These activities will ultimately allow to drastically expand our arsenal of functionalities in the design of novel molecules and our capacity to reliably produce them."
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