Abstract
Lasso peptides are unique in that the tail of the lasso peptide threads through its macrolactam ring. The unusual structure and biological activity of lasso peptides have generated increased interest from the scientific community in recent years. Because of this, many new
types of lasso peptides have been discovered. These peptides can be synthesized by microorganisms efficiently, and yet, their chemical assembly is challenging. Herein, we investigated the possibility of high pressure inducing the cyclization of linear precursors of lasso
peptides. Unlike other molecules like rotaxanes which mechanically interlock at high pressure, the threaded lasso peptides did not form, even at pressures the high pressure up to 14000 kbar.
Original language | English (US) |
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Pages (from-to) | e0234901 |
Journal | PLOS ONE |
Volume | 15 |
Issue number | 6 |
DOIs | |
State | Published - Jun 24 2020 |
Bibliographical note
KAUST Repository Item: Exported on 2020-10-01Acknowledgements: This work was supported by Grant No.UMO-2015/19/B/ST5/00659 from the National Science Centre, Poland https://www.ncn.gov.pl/ The co-authors: Łukasz Jaremko, Mariusz Jaremko, Priyadharshni Rajagopal and Kacper Szczepski are grateful to King Abdullah University of Science and Technology (KAUST) for financial support. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.