title: In vitro selection of functional lantipeptides.
abstract: In this report we present a method to identify functional artificial lantipeptides. In vitro translation coupled with an enzyme-free protocol for posttranslational modification allows preparation of more than 10(11) different lanthionine containing peptides. This diversity can be searched for functional molecules using mRNA-lantipeptide display. We validated this approach by isolating binders toward Sortase A, a transamidase which is required for virulence of Staphylococcus aureus. The interaction of selected lantipeptides with Sortase A is highly dependent on the presence of a (2S,6R)-lanthionine in the peptide and an active conformation of the protein.
authors.affiliation: Department of Physical Biochemistry, Max Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.
authors.forename: Frank T
authors.initials: FT
authors.lastname: Hofmann
authors.forename: Jack W
authors.initials: JW
authors.lastname: Szostak
authors.forename: Florian P
authors.initials: FP
authors.lastname: Seebeck
mesh_terms: D000595:Amino Acid Sequence; D019881:Aminoacyltransferases / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D003546:Cysteine Endopeptidases / Q000378:metabolism; D015723:Gene Library; D010455:Peptides / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D015202:Protein Engineering / Q000379:methods*
chemical_list: D001426:Bacterial Proteins; D010455:Peptides; D019881:Aminoacyltransferases; C120542:sortase A; D003546:Cysteine Endopeptidases