Work

In Vitro Selection of Functional Lantipeptides

Year: 2012

Type: article

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.

Source: Journal of the American Chemical Society

DOI: 10.1021/ja302082d

Authors: Frank T. Hofmann, Jack W. Szostak, Florian P. Seebeck

Institutions: Max Planck Institute of Molecular Physiology, Howard Hughes Medical Institute, Massachusetts General Hospital, Center for Computational and Integrative Biology, Massachusetts General Hospital, University of Basel

Language: English

Topic: Chemical Synthesis and Analysis

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $4,500

Funders: Howard Hughes Medical Institute, International Max Planck Research School for Environmental, Cellular and Molecular Microbiology