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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Javahishvili, Tsotne Reed, Sean A. Schultz, Peter G. Zhang, Yuhan Luo, Xiaozhou Xuan, Weimin Yang, Peng-yu Young, Travis S. Wang, Chen Liu, Tao Wang, Rongsheng E. Zambaldo, Claudio |
| Description | Author Affiliation: Luo X ( Department of Chemistry, The Scripps Research Institute, La Jolla, CA 92037); Zambaldo C ( Department of Chemistry, The Scripps Research Institute, La Jolla, CA 92037); Liu T ( Department of Chemistry, The Scripps Research Institute, La Jolla, CA 92037); Zhang Y ( Department of Biology, California Institute for Biomedical Research, La Jolla, CA 92037.); Xuan W ( Department of Chemistry, The Scripps Research Institute, La Jolla, CA 92037); Wang C ( Department of Biology, California Institute for Biomedical Research, La Jolla, CA 92037.); Reed SA ( Department of Chemistry, The Scripps Research Institute, La Jolla, CA 92037); Yang PY ( Department of Chemistry, The Scripps Research Institute, La Jolla, CA 92037); Wang RE ( Department of Biology, California Institute for Biomedical Research, La Jolla, CA 92037.); Javahishvili T ( Department of Biology, California Institute for Biomedical Research, La Jolla, CA 92037.); Schultz PG ( Department of Chemistry, The Scripps Research Institute, La Jolla, CA 92037); Young TS ( Department of Biology, California Institute for Biomedical Research, La Jolla, CA 92037 schultz@scripps.edu tyoung@calibr.org.); |
| Abstract | Thiopeptides are a subclass of ribosomally synthesized and posttranslationally modified peptides (RiPPs) with complex molecular architectures and an array of biological activities, including potent antimicrobial activity. Here we report the generation of thiopeptides containing noncanonical amino acids (ncAAs) by introducing orthogonal amber suppressor aminoacyl-tRNA synthetase/tRNA pairs into a thiocillin producer strain of Bacillus cereus .We demonstrate that thiopeptide variants containing ncAAs with bioorthogonal chemical reactivity can be further postbiosynthetically modified with biophysical probes, including fluorophores and photo-cross-linkers. This work allows the site-specific incorporation of ncAAs into thiopeptides to increase their structural diversity and probe their biological activity; similar approaches can likely be applied to other classes of RiPPs. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 13 |
| Volume Number | 113 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2016-04-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Amino Acids Chemistry Peptides Amino Acid Substitution Genetics Metabolism Bacillus Cereus Molecular Structure Mutagenesis, Site-Directed Protein Engineering Protein Processing, Post-Translational Recombinant Proteins Tandem Mass Spectrometry Research Support, N.I.H., Extramural Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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