22488-05-7Relevant articles and documents
SYNTHESIS OF 2Z,6Z,10Z,14E,18E-FARNESYLFARNESOL
Moiseenkov, A. M.,Novikova, M. A.,Polunin, E. V.,Torgova, S. I.
, p. 1407 - 1411 (1983)
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Nozoe,S.,Morisaki,M.
, p. 1319 - 1320 (1969)
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Synergistic factors ensue high expediency in the synthesis of menaquinone [K2] analogue MK-6: Application to access an efficient one-pot protocol to MK-9
Yerramsetti, Nanaji,Dampanaboina, Lavanya,Mendu, Venugopal,Battula, Satyanarayana
, (2020/11/12)
Here we report a practical and efficient method for the synthesis of menaquinone vitamin (K2) analog MK-6 in all trans forms through “1 + 5 convergent synthetic approach” of pentaprenyl chloride with monoprenyl menadione derivative. In the synergistic factors, less efficient leaving group/more efficient nucleophile (Cl) in the substrate makes it more prominent reaction by eliminating all Sn2’ side reaction products. Further, the addition of acetic acid in the last step (desulfonation) of reaction sequence removes the limitations of the reactions in terms of cyclized side product (multiple reactions of pentaprenyl alcohol with Et3B), byproduct (Et3B, incendiary compound) formations and their interruption in the tricky purification processes. The utility of this method was further extended to find an efficient one-pot synthesis to MK-9 to the gram scale synthesis. This approach is economical and efficient and avoids the awkward chromatographic separation processes.
GERANYLGERANYLACETONE DERIVATIVES
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, (2013/04/13)
Provided herein are geranylgeranylacetone derivatives and methods of using them.
Staphylococcus aureus penicillin-binding protein 2 can use depsi-lipid ii derived from vancomycin-resistant strains for cell wall synthesis
Nakamura, Jun,Yamashiro, Hidenori,Miya, Hiroto,Nishiguchi, Kenzo,Maki, Hideki,Arimoto, Hirokazu
, p. 12104 - 12112 (2013/09/23)
Vancomycin-resistant Staphylococcus aureus (S. aureus) (VRSA) uses depsipeptide-containing modified cell-wall precursors for the biosynthesis of peptidoglycan. Transglycosylase is responsible for the polymerization of the peptidoglycan, and the penicillin-binding protein 2 (PBP2) plays a major role in the polymerization among several transglycosylases of wild-type S. aureus. However, it is unclear whether VRSA processes the depsipeptide-containing peptidoglycan precursor by using PBP2. Here, we describe the total synthesis of depsi-lipid I, a cell-wall precursor of VRSA. By using this chemistry, we prepared a depsi-lipid II analogue as substrate for a cell-free transglycosylation system. The reconstituted system revealed that the PBP2 of S. aureus is able to process a depsi-lipid II intermediate as efficiently as its normal substrate. Moreover, the system was successfully used to demonstrate the difference in the mode of action of the two antibiotics moenomycin and vancomycin. Copyright
