Cover Feature: A Chemical Biology Approach to Understanding Molecular Recognition of Lipid II by Nisin(1–12): Synthesis and NMR Ensemble Analysis of Nisin(1–12) and Analogues (Chem. Eur. J. 64/2019). Issue 64 (10th October 2019)

• Record Type: Journal Article
• Authors: Dickman, Rachael; Danelius, Emma; Mitchell, Serena A.; Hansen, D. Flemming; Erdélyi, Máté; Tabor, Alethea B.
• Is Part Of: Chemistry. Volume 25:Issue 64(2019)
• Page Start: 14478
• Page End: 14478
• Publication Date: 2019-10-10
• Subjects: antibiotics -- cyclic peptides -- lantibiotics -- NMR spectroscopy -- solid phase synthesis; Chemistry -- Periodicals; 540
• DOI: 10.1002/chem.201903848
• Languages: English
• ISSNs: 0947-6539

Abstract

Abstract : Lipid II recognition : Analogues of the bicyclic N‐terminal region of the lantibiotic nisin, residues 1–12, were synthesised. In order to analyse how this region of the peptide binds to its target, the pyrophosphate moiety of lipid II, NMR ensemble analysis of the wild‐type peptide and one of the synthetic analogues was carried out. This revealed that the two rings are pre‐organised to an extent for binding to the pyrophosphate group. A high degree of flexibility exhibited in the central amide bond joining the two rings enables the two rings to switch between an "open" structure and a "cage" capable of binding to the pyrophosphate. More information can be found in the Full Paper by M. Erdélyi, A. B. Tabor et al. on page 14572 .