367276-31-1Relevant academic research and scientific papers
Insights into the Mechanism of Action of the Two-Peptide Lantibiotic Lacticin 3147
Bakhtiary, Alireza,Cochrane, Stephen A.,Mercier, Pascal,McKay, Ryan T.,Miskolzie, Mark,Sit, Clarissa S.,Vederas, John C.
supporting information, p. 17803 - 17810 (2017/12/26)
Lacticin 3147 is a two peptide lantibiotc (LtnA1 and LtnA2) that displays nanomolar activity against many Gram-positive bacteria. Lacticin 3147 may exert its antimicrobial effect by several mechanisms. Isothermal titration calorimetry experiments show that only LtnA1 binds to the peptidoglycan precursor lipid II, which could inhibit peptidoglycan biosynthesis. An experimentally supported model of the resulting complex suggests that the key binding partners are the C-terminus of LtnA1 and pyrophosphate of lipid II. A combination of in vivo and in vitro assays indicates that LtnA1 and LtnA2 can induce rapid membrane lysis without the need for lipid II binding. However, the presence of lipid II substantially increases the activity of lacticin 3147. Furthermore, studies with synthetic LtnA2 analogues containing either desmethyl- or oxa-lanthionine rings confirm that the precise geometry of these rings is essential for this synergistic activity.
The first total synthesis of lipid II: The final monomeric intermediate in bacterial cell wall biosynthesis
VanNieuwenhze, Michael S.,Mauldin, Scott C.,Zia-Ebrahimi, Mohammad,Winger, Brian E.,Hornback, William J.,Saha, Shankar L.,Aikins, James A.,Blaszczak, Larry C.
, p. 3656 - 3660 (2007/10/03)
Bacterial peptidoglycan is composed of a network of β-[1,4]-linked glyan strands that are crosslinked through pendant peptide chains. The final product, the murein sacculus, is a single, covalently closed macromolecule that precisely defines the size and
