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Search for "lipid II" in Full Text gives 8 result(s) in Beilstein Journal of Organic Chemistry.
Chemical glycobiology
Beilstein J. Org. Chem. 2025, 21, 8–9, doi:10.3762/bjoc.21.2
- glycan assembly [9]. Target-directed synthetic strategies are being developed by Reihill et al. [10] and Karak et al. [11], exploring the syntheses of the linker-displaying, sulfated TF disaccharide and lipid II analogues, respectively. The direct application of synthetic glycans is shown by Fan et al
Chemical structure metagenomics of microbial natural products: surveying nonribosomal peptides and beyond
Beilstein J. Org. Chem. 2024, 20, 3050–3060, doi:10.3762/bjoc.20.253
- of action (MOA) (e.g., membrane lysis and depolarization) [30][34] and specific MOA (e.g., dysregulation of ClpP protease [33], inhibition of topoisomerase I/II [36][68], blocking lipid II transport by flippase [29], sequestration of cell wall biosynthetic intermediate C55-(di)phosphate, etc.) [35
Discovery of antimicrobial peptides clostrisin and cellulosin from Clostridium: insights into their structures, co-localized biosynthetic gene clusters, and antibiotic activity
Beilstein J. Org. Chem. 2024, 20, 1800–1816, doi:10.3762/bjoc.20.159
- Mycobacterium tuberculosis. The effects of some of these peptides are attributed to their affinity for the lipid II component of Gram-positive bacterial cell walls [25]. Additionally, there have been reports of lantibiotics such as CMB001 displaying activity against resistant Gram-negative bacteria, including
Optimizations of lipid II synthesis: an essential glycolipid precursor in bacterial cell wall synthesis and a validated antibiotic target
Beilstein J. Org. Chem. 2024, 20, 220–227, doi:10.3762/bjoc.20.22
- Milandip Karak Cian R. Cloonan Brad R. Baker Rachel V. K. Cochrane Stephen A. Cochrane School of Chemistry and Chemical Engineering, Queen's University Belfast, David Keir Building, Stranmillis Road, Belfast, BT9 5AG, UK 10.3762/bjoc.20.22 Abstract Lipid II is an essential glycolipid found in
- bacteria. Accessing this valuable cell wall precursor is important both for studying cell wall synthesis and for studying/identifying novel antimicrobial compounds. Herein, we describe optimizations to the modular chemical synthesis of lipid II and unnatural analogues. In particular, the glycosylation step
- analogues through the incorporation of alternative building blocks at different stages of synthesis. Keywords: chemical glycosylation; lipid II; peptidoglycan; polyprenyls; total synthesis; Introduction Lipid II (Figure 1) is an essential bacterial glycolipid involved in peptidoglycan biosynthesis [1]. It
Biochemical and structural characterisation of the second oxidative crosslinking step during the biosynthesis of the glycopeptide antibiotic A47934
Beilstein J. Org. Chem. 2016, 12, 2849–2864, doi:10.3762/bjoc.12.284
- enables them to bind to the dipeptide terminus of the peptidoglycan precursor lipid II [1][2]. This three-dimensional structure is generated by the high degree of crosslinking exhibited by the glycopeptide antibiotics: in the case of the two most widely known natural examples (vancomycin and teicoplanin
Enduracididine, a rare amino acid component of peptide antibiotics: Natural products and synthesis
Beilstein J. Org. Chem. 2016, 12, 2325–2342, doi:10.3762/bjoc.12.226
- using traditional techniques. Teixobactin (17) exhibits bactericidal activity through binding of Lipid II, a precursor of peptidoglycan, and therefore shows great potential as the foundation for discovery of a new generation of antibiotics to overcome the development of antimicrobial resistance
- which involves binding to Lipid II, inhibiting one of the membrane-associated steps of peptidoglycan biosynthesis [43][44]. Analogues of teixobactin (17) have undergone biological testing and results show that the L-allo-enduracididine (3, blue, Figure 7) residue is important for potent antibacterial
Muraymycin nucleoside-peptide antibiotics: uridine-derived natural products as lead structures for the development of novel antibacterial agents
Beilstein J. Org. Chem. 2016, 12, 769–795, doi:10.3762/bjoc.12.77
- furnish lipid II (Figure 4, product of step C). This building block is then transported to the extracellular side of the membrane. It is speculated that there might be some kind of 'flippase' involved but this particular step is still unclear and requires further investigation [55]. On the extracellular
- compounds were able to inhibit lipid II formation. These active compounds are discussed in the section on structure–activity relationship (SAR) studies. In 2005, Ichikawa, Matsuda et al. reported the synthesis of (+)-caprazol [90][91][92] which contains the same uridine-derived core structure as the
- inhibition of lipid II formation at 6.25 μg/mL, which is comparable to muraymycin C1. Good activity was also found for hydantoin derivative 77 with the 4-FC6H4 substituent, showing inhibition of lipid II formation at 25 μg/mL. The only N-alkylated derivative inhibiting in the same order of magnitude was 83
Modulating the activity of short arginine-tryptophan containing antibacterial peptides with N-terminal metallocenoyl groups
Beilstein J. Org. Chem. 2012, 8, 1753–1764, doi:10.3762/bjoc.8.200
- activities of these RW-based synAMPs and their organometallic conjugates into perspective, two reference peptides were included, i.e., membrane-targeting gramicidin S derivative GS(K2Y2) and cell wall precursor lipid II-targeting vancomycin. For the calculations of the MIC values in µM, molecular weights of
- ) and their metallocene-derivatives (right); the lower row shows the structure of pore-forming gramicidin S derivative GS(K2Y2) (left) and lipid II-binding cell wall biosynthesis inhibitor vancomycin (right). Bactericidal activity of (RW)3 against S. aureus 133 (panel A and D) or B. megaterium (panel B
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