41355-95-7Relevant academic research and scientific papers
Synthesis of Bacterial-Derived Peptidoglycan Cross-Linked Fragments
Mashayekh, Siavash,Bersch, Klare L.,Ramsey, Jared,Harmon, Thomas,Prather, Benjamin,Genova, Lauren A.,Grimes, Catherine L.
supporting information, p. 16243 - 16253 (2020/11/13)
Peptidoglycan (PG) is the core structural motif of the bacterial cell wall. Fragments released from the PG serve as fundamental recognition elements for the immune system. The structure of the PG, however, encompasses a variety of chemical modifications among different bacterial species. Here, the applicability of organic synthetic methods to address this chemical diversity is explored, and the synthesis of cross-linked PG fragments, carrying biologically relevant amino acid modifications and peptide cross-linkages, is presented using solution and solid phase approaches.
Monosaccharide inhibitors targeting carbohydrate esterase family 4 de-N-acetylases
DiFrancesco, Benjamin R.,Morrison, Zachary A.,Nitz, Mark
, p. 5631 - 5643 (2018/10/24)
The Carbohydrate Esterase family 4 contains virulence factors which modify peptidoglycan and biofilm-related exopolysaccharides. Despite the importance of this family of enzymes, a potent mechanism-based inhibition strategy has yet to emerge. Based on the postulated tridentate binding mode of the tetrahedral de-N-acetylation intermediate, GlcNAc derivatives bearing metal chelating groups at the 2 and 3 positions were synthesized. These scaffolds include 2-C phosphonate, 2-C sulfonamide, 2-thionoacetamide warheads as well as derivatives bearing thiol, amine and azide substitutions at the 3-position. The inhibitors were assayed against a representative peptidoglycan deacetylase, Pgda from Streptococcus pneumonia, and a representative biofilm-related exopolysaccharide deacetylase, PgaB from Escherichia coli. Of the inhibitors evaluated, the 3-thio derivatives showed weak to moderate inhibition of Pgda. The strongest inhibitor was benzyl 2,3-dideoxy-2-thionoacetamide-3-thio-β-D-glucoside, whose inhibitory potency showed an unexpected dependence on metal concentration and was found to have a partial mixed inhibition mode (Ki = 2.9 ± 0.6 μM).
Synthesis and antimicrobial activity of 6-sulfo-6-deoxy-D-glucosamine and its derivatives
Skarbek, Kornelia,Gabriel, Iwona,Szweda, Piotr,Wojciechowski, Marek,Khan, Muna A.,G?rke, Boris,Milewski, S?awomir,Milewska, Maria J.
, p. 79 - 87 (2017/06/20)
6-Sulfo-6-deoxy-D-glucosamine (GlcN6S), 6-sulfo-6-deoxy-D-glucosaminitol (ADGS) and their N-acetyl and methyl ester derivatives have been synthesized and tested as inhibitors of enzymes catalyzing reactions of the UDP-GlcNAc pathway in bacteria and yeasts
Chemoenzymatic Synthesis of 4-Fluoro-N-Acetylhexosamine Uridine Diphosphate Donors: Chain Terminators in Glycosaminoglycan Synthesis
Schultz, Victor L.,Zhang, Xing,Linkens, Kathryn,Rimel, Jenna,Green, Dixy E.,Deangelis, Paul L.,Linhardt, Robert J.
, p. 2243 - 2248 (2017/02/26)
Unnatural uridine diphosphate (UDP)-sugar donors, UDP-4-deoxy-4-fluoro-N-acetylglucosamine (4FGlcNAc) and UDP-4-deoxy-4-fluoro-N-acetylgalactosamine (4FGalNAc), were prepared using both chemical and chemoenzymatic syntheses relying on N-acetylglucosamine-
Synthesis of lipo-chitooligosaccharide analogues and their interaction with LYR3, a high affinity binding protein for Nod factors and Myc-LCOs
Berthelot, Nathan,Brossay, Antoine,Gasciolli, Virginie,Bono, Jean-Jacques,Baron, Aurélie,Beau, Jean-Marie,Urban, Dominique,Boyer, Fran?ois-Didier,Vauzeilles, Boris
, p. 7802 - 7812 (2017/10/06)
Lipo-chitotetrasaccharide analogues where one central GlcNAc residue was replaced by a triazole unit have been synthesized from a derivative obtained by chitin depolymerization and a functionalized N-acetyl-glucosamine via the copper-catalyzed azide-alkyn
Sugar derived alkamine catalytic imine reduction method
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Paragraph 0038; 0039, (2016/10/07)
The invention discloses a method used for catalytic reduction of imine with saccharide-derivatized amino alcohol. According to the method, imine is taken as a substrate. The method comprises following steps: 1) imine and saccharide-derivatized amino alcohol are dissolved in an organic solvent I, wherein molar ratio of imine to saccharide-derivatized amino alcohol ranges from 100:1-20; 2) trichlorosilane with 1.5 to 5 times equivalent weights is added into a solution obtained via step 1) dropwise, an obtained mixture is stirred and reacted for 12 to 36h at a temperature of -20 to 40 DEG C, and a saturated sodium bicarbonate solution is used for quenching; 3) a material obtained via step 2) is extracted with an organic solvent II, and is subjected to column chromatography isolation so as to obtain amine compounds.
Chemo-enzymatic approach to access diastereopure α-substituted GlcNAc derivatives
Wang, Su-Yan,Laborda, Pedro,Lu, Ai-Min,Wang, Meng,Duan, Xu-Chu,Liu, Li,Voglmeir, Josef
, p. 423 - 434 (2017/08/23)
The formation of diastereopure α-substituted GlcNAc derivatives in a simple and straightforward way is a challenging task. Herein, we report the chemical synthesis of diastereomeric α/β-substituted GlcNAc derivatives under non-anhydrous atmosphere using u
A robust synthesis of N-glycolyl muramyl dipeptide via azidonitration/reduction
Xing, Shuo,Gleason, James L.
, p. 1515 - 1520 (2015/01/30)
A novel synthetic route leading to N-glycolyl muramyl dipeptide (MDP), a bacterial glycopeptide of particular interest in studies of nucleotide-binding oligomerization domain-containing protein 2 (NOD2), is described. The synthetic strategy hinges on the alkylation of benzylidene-protected glucal with 2-bromopropionic acid and thus circumvents a challenging and non-reproducible SN2 step at the C-3 position of glucosamine derivatives. The subsequent sequence includes an azidonitration and an unusual azide reduction/acylation step via an aza ylide/oxaphospholidine intermediate. This approach generates a protected N-glycolyl MDP that can be either subjected to a one-step global deprotection or differentially deprotected to obtain further derivatives.
Order of reactivity of OH/NH groups of glucosamine hydrochloride and N -Acetyl glucosamine toward benzylation using NaH/BnBr in DMF
Ali, Stacy P.,Jalsa, Nigel Kevin
, p. 185 - 196 (2014/06/09)
The order of reactivity of OH and NH groups of glucosamine hydrochloride (GlcNH2HCl) and N-acetyl glucosamine (GlcNAc) toward benzylation with NaH/BnBr in DMF was investigated. For GlcNH2.HCl, benzyl groups were introduced in the order of N-Bn > N-Bn2 > 1-O-Bn > 6-O-Bn > 4-O-Bn > 3-O-Bn; for GlcNAc, benzyl groups were introduced in the order of 1-O-Bn > 6-O-Bn > 4-O-Bn > 3-O-Bn > N-Bn. A range of partially benzylated 2-N,N′-dibenzyl glucopyranosides and GlcNAc derivatives were obtained in a single step. Taylor & Francis Group, LLC.
Chondroitin-4-O-sulfatase from Bacteroides thetaiotaomicron: Exploration of the substrate specificity
Malleron, Annie,Benjdia, Alhosna,Berteau, Olivier,Le Narvor, Christine
scheme or table, p. 96 - 99 (2012/07/01)
Bacterial sulfatases can be good tools to increase the molecular diversity of glycosaminoglycan synthetic fragments. A chondroitin 4-O-sulfatase from the human commensal bacterium Bacteroides thetaiotaomicron has recently been identified and expressed. In order to use this enzyme for synthetic purposes, the minimal structure required for its activity has been determined. For that, four 4-O-sulfated monosaccharides and one 4-O-sulfated disaccharide have been synthesized and used as substrates with the sulfatase. The minimum structure was shown to be a disaccharide but in contrast to the natural substrate, which must have a 4,5-insaturation, the enzyme accepts as substrate, a disaccharide with a saturated glucuronic acid at the non-reducing end and even a glucopyranosyl moiety without the carboxylic acid functionality.
