Elsayed, Somayah S., Trusch, Franziska, Deng, Hai, Raab, Andrea, Prokes, Ivan, Busarakam, Kanungnid, Asenjo, Juan A., Andrews, Barbara A., van West, Pieter, Bull, Alan T., and others. (2015) Chaxapeptin, a Lasso Peptide from ExtremotolerantStreptomyces leeuwenhoekiiStrain C58 from the Hyperarid Atacama Desert. The Journal of Organic Chemistry, 80 (20). pp. 10252-10260. ISSN 0022-3263. (doi:10.1021/acs.joc.5b01878) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:51195)
| The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. | |
| Official URL: http://doi.org/10.1021/acs.joc.5b01878 |
|
Abstract
Lasso peptides are ribosomally synthesized and post-translationally modified peptides (RiPPs) that possess a unique “lariat knot” structural motif. Genome mining-targeted discovery of new natural products from microbes obtained from extreme environments has led to the identification of a gene cluster directing the biosynthesis of a new lasso peptide, designated as chaxapeptin 1, in the genome of Streptomyces leeuwenhoekii strain C58 isolated from the Atacama Desert. Subsequently, 1 was isolated and characterized using high-resolution electrospray ionization mass spectrometry and nuclear magnetic resonance methods. The lasso nature of 1 was confirmed by calculating its nuclear Overhauser effect restraint-based solution structure. Chaxapeptin 1 displayed a significant inhibitory activity in a cell invasion assay with human lung cancer cell line A549.
| Item Type: | Article |
|---|---|
| DOI/Identification number: | 10.1021/acs.joc.5b01878 |
| Subjects: | Q Science |
| Institutional Unit: | Schools > School of Natural Sciences > Biosciences |
| Former Institutional Unit: |
Divisions > Division of Natural Sciences > Biosciences
|
| Depositing User: | Susan Davies |
| Date Deposited: | 22 Oct 2015 10:59 UTC |
| Last Modified: | 20 May 2025 09:20 UTC |
| Resource URI: | https://kar.kent.ac.uk/id/eprint/51195 (The current URI for this page, for reference purposes) |
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https://orcid.org/0000-0001-6223-7722
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