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      In Vitro Selection of Functional Lantipeptides

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          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 (2 S,6 R)-lanthionine in the peptide and an active conformation of the protein.

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          Stapled peptides for intracellular drug targets.

          J Hilinski, Gregory L. Verdine (2011)
          Proteins that engage in intracellular interactions with other proteins are widely considered among the most biologically appealing yet chemically intractable targets for drug discovery. The critical interaction surfaces of these proteins typically lack the deep hydrophobic involutions that enable potent, selective targeting by small organic molecules, and their localization within the cell puts them beyond the reach of protein therapeutics. Considerable interest has therefore arisen in next-generation targeting molecules that combine the broad target recognition capabilities of protein therapeutics with the robust cell-penetrating ability of small molecules. One type that has shown promise in early-stage studies is hydrocarbon-stapled α-helical peptides, a novel class of synthetic miniproteins locked into their bioactive α-helical fold through the site-specific introduction of a chemical brace, an all-hydrocarbon staple. Stapling can greatly improve the pharmacologic performance of peptides, increasing their target affinity, proteolytic resistance, and serum half-life while conferring on them high levels of cell penetration through endocytic vesicle trafficking. Here, we discuss considerations crucial to the successful design and evaluation of potent stapled peptide interactions, our intention being to facilitate the broad application of this technology to intractable targets of both basic biologic interest and potential therapeutic value. Copyright © 2012 Elsevier Inc. All rights reserved.
          Article 0 comments Cited 102 times – based on 0 reviews     Review now
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            Biosynthesis, immunity, regulation, mode of action and engineering of the model lantibiotic nisin.

            J Lubelski, R Rink, R Khusainov … (2008)
            This review discusses the state-of-the-art in molecular research on the most prominent and widely applied lantibiotic, i.e., nisin. The developments in understanding its complex biosynthesis and mode of action are highlighted. Moreover, novel applications arising from engineering either nisin itself, or from the construction of totally novel dehydrated and/or lanthionine-containing peptides with desired bioactivities are described. Several challenges still exist in understanding the immunity system and the unique multiple reactions occurring on a single substrate molecule, carried out by the dehydratase NisB and the cyclization enzyme NisC. The recent elucidation of the 3-D structure of NisC forms the exciting beginning of further 3-D-structure determinations of the other biosynthetic enzymes, transporters and immunity proteins. Advances in achieving in vitro activities of lanthionine-forming enzymes will greatly enhance our understanding of the molecular characteristics of the biosynthesis process, opening up new avenues for developing unique and novel biocatalytic processes.
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              An iron-regulated sortase anchors a class of surface protein during Staphylococcus aureus pathogenesis.

              S. Mazmanian, H Ton-That, K. Su … (2002)
              Sortase (SrtA), an enzyme that anchors surface proteins to the cell wall of Gram-positive bacteria, cleaves sorting signals at the LPXTG motif. We have identified a second sortase (SrtB) in the Gram-positive pathogen Staphylococcus aureus that is required for anchoring of a surface protein with a NPQTN motif. Purified SrtB cleaves NPQTN-bearing peptides in vitro, and a srtB mutant is defective in the persistence of animal infections. srtB is part of an iron-regulated locus called iron-responsive surface determinants (isd), which also contains a ferrichrome transporter and surface proteins with NPQTN and LPXTG motifs. Cell wall-anchored surface proteins and the isd locus seem involved in a novel mechanism of iron acquisition that is important for bacterial pathogenesis.
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                Author and article information

                Journal
                Journal ID (nlm-ta): J Am Chem Soc
                Journal ID (iso-abbrev): J. Am. Chem. Soc
                Journal ID (publisher-id): ja
                Journal ID (coden): jacsat
                Title: Journal of the American Chemical Society
                Publisher: American Chemical Society
                ISSN (Print): 0002-7863
                ISSN (Electronic): 1520-5126
                Publication date (Electronic): 30 April 2012
                Publication date (Print): 16 May 2012
                Volume: 134
                Issue: 19
                Pages: 8038-8041
                Affiliations
                [† ]Department of Physical Biochemistry, simpleMax Planck Institute of Molecular Physiology , Otto-Hahn-Strasse 11, 44227 Dortmund, Germany
                [‡ ]Howard Hughes Medical Institute and Department of Molecular Biology and Center for Computational and Integrative Biology, Simches Research Center, simpleMassachusetts General Hospital , 185 Cambridge Street, Boston, Massachusetts 02114, United States
                [§ ]Department for Chemistry, simpleUniversity of Basel , St. Johanns-Ring 19, 4056, Basel, Switzerland
                Author notes
                Article
                DOI: 10.1021/ja302082d
                PMC ID: 3353655
                PubMed ID: 22545861
                SO-VID: b8a45ffa-ab69-486b-a9cb-b9a8b739a067
                Copyright © Copyright © 2012 American Chemical Society
                License:

                This is an open-access article distributed under the ACS AuthorChoice Terms & Conditions. Any use of this article, must conform to the terms of that license which are available at http://pubs.acs.org.

                History
                Date received : 02 March 2012
                Date: 03 May 2012
                Date: 16 May 2012
                Date: 30 April 2012
                Categories
                Subject: Communication
                Custom metadata
                document-id-old-9 ja302082d
                document-id-new-14 ja-2012-02082d
                ccc-price

                ScienceOpen disciplines: Chemistry
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                ScienceOpen disciplines: Chemistry

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