title: Post-translational modification of genetically encoded polypeptide libraries.
abstract: The genetic encoding of polypeptides with biological display systems enables the facile generation and screening of very large combinatorial libraries of molecules. By post-translationally modifying the encoded polypeptides, chemically and structurally more diverse molecules beyond linear amino acid polymers can be generated. The first post-translational modification applied to encoded polypeptides, the oxidation of cysteine residues to form disulfide bridges, is a natural one and was used to cyclise short peptides soon after the invention of phage display. Recently a range of non-natural chemical strategies for the post-translational modification of encoded polypeptide repertoires were applied to generate optical biosensors, semisynthetic polypeptides, peptide-drug conjugates, redox-insensitive monocyclic peptides or multicyclic peptides, and these strategies are reviewed in this article.
authors.affiliation: Institute of Chemical Sciences and Engineering, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland.
authors.forename: Alessandro
authors.initials: A
authors.lastname: Angelini
authors.forename: Christian
authors.initials: C
authors.lastname: Heinis
mesh_terms: D020650:Combinatorial Chemistry Techniques; D006801:Humans; D019151:Peptide Library; D010455:Peptides / Q000737:chemistry* / Q000235:genetics; D015202:Protein Engineering; D011499:Protein Processing, Post-Translational
chemical_list: D019151:Peptide Library; D010455:Peptides