99409-33-3Relevant academic research and scientific papers
Ionic-liquid supported rapid synthesis of an: N -glycan core pentasaccharide on a 10 g scale
Li, Wei,Gao, Yu,Li, Qing,Li, Zhong-Jun
supporting information, p. 4720 - 4727 (2018/07/06)
A new and efficient Ionic Liquid-Supported Oligosaccharide Synthesis (ILSOS) strategy for an N-linked core pentasaccharide on a 10 g scale is reported. This new ILSOS includes a new spacer for an IL support, a new tagging strategy, and fast, efficient and orthogonal removal of the ionic-liquid support, producing the N-linked core pentasaccharide with direct applicability potential in a short time, with high yield and on a large gram scale.
'Naked' and hydrated conformers of the conserved core pentasaccharide of N-linked glycoproteins and its building blocks
Barry, Conor S.,Cocinero, Emilio J.,Carcabal, Pierre,Gamblin, David P.,Stanca-Kaposta, E. Cristina,Remmert, Sarah M.,Fernandez-Alonso, Maria C.,Rudic, Svemir,Simons, John P.,Davis, Benjamin G.
supporting information, p. 16895 - 16903 (2013/12/04)
N-glycosylation of eukaryotic proteins is widespread and vital to survival. The pentasaccharide unit -Man3GlcNAc2- lies at the protein-junction core of all oligosaccharides attached to asparagine side chains during this process. Although its absolute conservation implies an indispensable role, associated perhaps with its structure, its unbiased conformation and the potential modulating role of solvation are unknown; both have now been explored through a combination of synthesis, laser spectroscopy, and computation. The proximal -GlcNAc-GlcNAc- unit acts as a rigid rod, while the central, and unusual, -Man-β-1,4-GlcNAc- linkage is more flexible and is modulated by the distal Man-α-1,3- and Man-α-1,6- branching units. Solvation stiffens the 'rod' but leaves the distal residues flexible, through a β-Man pivot, ensuring anchored projection from the protein shell while allowing flexible interaction of the distal portion of N-glycosylation with bulk water and biomolecular assemblies.
Combining weak affinity chromatography, NMR spectroscopy and molecular simulations in carbohydrate-lysozyme interaction studies
Landstroem, Jens,Bergstroem, Maria,Hamark, Christoffer,Ohlson, Sten,Widmalm, Goeran
, p. 3019 - 3032 (2012/05/07)
By examining the interactions between the protein hen egg-white lysozyme (HEWL) and commercially available and chemically synthesized carbohydrate ligands using a combination of weak affinity chromatography (WAC), NMR spectroscopy and molecular simulations, we report on new affinity data as well as a detailed binding model for the HEWL protein. The equilibrium dissociation constants of the ligands were obtained by WAC but also by NMR spectroscopy, which agreed well. The structures of two HEWL-disaccharide complexes in solution were deduced by NMR spectroscopy using 1H saturation transfer difference (STD) effects and transferred 1H,1H-NOESY experiments, relaxation-matrix calculations, molecular docking and molecular dynamics simulations. In solution the two disaccharides β-d-Galp-(1→4) -β-d-GlcpNAc-OMe and β-d-GlcpNAc-(1→4)-β-d-GlcpNAc-OMe bind to the B and C sites of HEWL in a syn-conformation at the glycosidic linkage between the two sugar residues. Intermolecular hydrogen bonding and CH/π-interactions form the basis of the protein-ligand complexes in a way characteristic of carbohydrate-protein interactions. Molecular dynamics simulations with explicit water molecules of both the apo-form of the protein and a ligand-protein complex showed structural change compared to a crystal structure of the protein. The flexibility of HEWL as indicated by a residue-based root-mean-square deviation analysis indicated similarities overall, with some residue specific differences, inter alia, for Arg61 that is situated prior to a flexible loop. The Arg61 flexibility was notably larger in the ligand-complexed form of HEWL. N,N′-Diacetylchitobiose has previously been observed to bind to HEWL at the B and C sites in water solution based on 1H NMR chemical shift changes in the protein whereas the disaccharide binds at either the B and C sites or the C and D sites in different crystal complexes. The present study thus highlights that protein-ligand complexes may vary notably between the solution and solid states, underscoring the importance of targeting the pertinent binding site(s) for inhibition of protein activity and the advantages of combining different techniques in a screening process. The Royal Society of Chemistry 2012.
Environmentally benign preparation of benzylidene acetal of carbohydrate derivatives in PEG 600
Sau, Abhijit,Misra, Anup Kumar
experimental part, p. 41 - 46 (2012/01/17)
An environmentally benign preparation of benzylidene acetal of carbohydrate derivatives catalyzed by HClO4-SiO2 in PEG 600 as solvent has been developed. Yields were excellent in every case. Copyright Taylor & Francis Group, LLC.
Chemoenzymatic synthesis of α2-3-sialylated carbohydrate epitopes
Huang, Shengshu,Yu, Hai,Chen, Xi
experimental part, p. 117 - 128 (2011/12/16)
Sialic acids are common terminal carbohydrates on cell surface. Together with internal carbohydrate structures, they play important roles in many physiological and pathological processes. In order to obtain α2-3-sialylated oligosaccharides, a highly efficient one-pot three-enzyme synthetic approach was applied. The P. multocida-α2-3-sialyltransferase (PmST1) involved in the synthesis was a multifunctional enzyme with extremely flexible donor and acceptor substrate specificities. Sialyltransferase acceptors, including type 1 structure (Galβ1-3GlcNAcβProN 3), type 2 structures (Galβ1-4GlcNAcβProN3 and 6-sulfo-Galβ1-4GlcNAcβProN3), type 4 structure (Galβ1-3GalNAcβProN3), type 3 or core 1 structure (Galβ1-3GalNAcαProN3) and human milk oligoscaccharide or lipooligosaccharide lacto-N-tetraose (LNT) (Galβ1-3GlcNAcβ1- 3Galβ1-4GlcβProN3), were chemically synthesized. They were then used in one-pot three-enzyme reactions with sialic acid precursor ManNAc or ManNGc, to synthesize a library of naturally occurring α2-3-linked sialosides with different internal sugar structures. The sialylated oligosaccharides obtained are valuable probes for their biological studies.
Sweets for catalysis - Facile optimisation of carbohydrate-based bis(oxazoline) ligands
Minuth, Tobias,Irmak, Mustafa,Groschner, Annika,Lehnert, Tobias,Boysen, Mike M. K.
experimental part, p. 997 - 1008 (2009/07/19)
A new type of carbohydrate-based bis(oxazoline) ligands was prepared from inexpensive D-glucosamine and tested in asymmetric cyclopropanation reactions. For optimisation, modified ligands with 3-O substituents of varying size and electronic properties were prepared as well as a 3-OH unprotected and a perpivaloylated derivative. All new ligands were tested in asymmetric cyclopropanation, revealing a strong dependence of enantioselectivity on steric demand and electronic properties of the 3-O residue. Also, a significant influence of the pyranose conformation, which is determined by the presence or absence of the cyclic acetal group, was observed. Thus, it was easily possible to tune the new carbohydrate bis(oxazoline) ligands to a given reaction.
Toward fully synthetic homogeneous β -human Follicle-Stimulating hormone (β -hFSH) with a biantennary N-linked dodecasaccharide. synthesis of β -hFSH with chitobiose units at the natural linkage sites
Nagorny, Pavel,Fasching, Bernhard,Li, Xuechen,Chen, Gong,Aussedat, Baptiste,Danishefsky, Samuel J.
supporting information; experimental part, p. 5792 - 5799 (2009/09/24)
A highly convergent synthesis of the sialic acid-rich biantennary N-linked glycan found in human glycoprotein hormones and its use in the synthesis of a fragment derived from the β -domain of human Follicle-Stimulating Hormone (hFSH) are described. The synthesis highlights the use of the Sinay radical glycosidation protocol for the simultaneous installation of both biantennary side-chains of the dodecasaccharide as well as the use of glycal chemistry to construct the tetrasaccharide core in an efficient manner. The synthetic glycan was used to prepare the glycosylated 20-27aa domain of the β -subunit of hFSH under a Lansbury aspartylation protocol. The proposed strategy for incorporating the prepared N-linked dodecasaccharide-containing 20-27aa domain into β -hFSH subunit was validated in the context of a model system, providing protected β -hFSH subunit functionalized with chitobiose at positions 7 and24.
A General and efficient route to 3-O-Modified carbohydrate bis(oxazoline) ligands
Minuth, Tobias,Boysen, Mike M. K.
scheme or table, p. 1483 - 1486 (2009/04/07)
An efficient route to derivatives of carbohydrate-based bis(oxazoline) ligands with 3-O substituents of varying steric demand is described. The synthesis of the new ligands proceeds via a thioglucoside key intermediate, the double cyclisation reaction to
Synthesis of deoxygenated disaccharide precursors for modified lipid II synthesis
Sun, De-Qun,Busson, Roger,Herdewijn, Piet
, p. 5158 - 5166 (2007/10/03)
The synthesis of novel deoxygenated disaccharide precursors for modified lipid II synthesis is described. The 3- and 4-deoxy-GlcNAc donors were obtained, respectively, by radical reduction of the iodo derivative by TBTH/AIBN and hydrogen reduction of the
Synthesis of the trisaccharide repeating unit of the O-antigen related to the enterohemorrhagic Escherichia coli type O26:H
Sarkar, Kakali,Mukherjee, Indrani,Roy, Nirmolendu
, p. 95 - 107 (2007/10/03)
L-Fucose was converted to the 2-azido-2-deoxy-L-fucose derivative, which together with the monosaccharide synthons prepared from L-rhamnose and D-glucosamine hydrochloride were utilized for the synthesis of the p-ethoxyphenyl glycoside of the trisaccharid
