Faculty of Chemistry, University of Wrocław, Wroclaw, Poland.
Biological and Environmental Sciences & Engineering Division (BESE), King Abdullah University of Science and Technology (KAUST), Thuwal, Saudi Arabia.
PLoS One. 2020 Jun 24;15(6):e0234901. doi: 10.1371/journal.pone.0234901. eCollection 2020.
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 14 000 kbar.
套索肽的独特之处在于，套索肽的尾部穿过大环内酯环。近年来，套索肽的不寻常结构和生物活性引起了科学界的极大兴趣。因此，已经发现了许多新型的套索肽。这些肽可以被微生物有效地合成，然而，它们的化学组装具有挑战性。在这里，我们研究了高压诱导套索肽线性前体环化的可能性。与其他在高压下机械互锁的分子（如轮烷）不同，即使在高达 14000 千巴的高压下，套索肽也没有形成。
