115533-35-2Relevant articles and documents
Picoloyl protecting group in synthesis: Focus on a highly chemoselective catalytic removal
Bandara, Mithila D.,Demchenko, Alexei V.,Geringer, Scott A.,Mannino, Michael P.
, p. 4863 - 4871 (2020/07/13)
The picoloyl ester (Pico) has proven to be a versatile protecting group in carbohydrate chemistry. It can be used for the purpose of stereocontrolling glycosylations via an H-bond-mediated Aglycone Delivery (HAD) method. It can also be used as a temporary protecting group that can be efficiently introduced and chemoselectively cleaved in the presence of practically all other common protecting groups used in synthesis. Herein, we will describe a new method for rapid, catalytic, and highly chemoselective removal of the picoloyl group using inexpensive copper(ii) or iron(iii) salts. This journal is
Regioselective Glycosylation Strategies for the Synthesis of Group Ia and Ib Streptococcus Related Glycans Enable Elucidating Unique Conformations of the Capsular Polysaccharides
Del Bino, Linda,Calloni, Ilaria,Oldrini, Davide,Raso, Maria Michelina,Cuffaro, Rossella,Ardá, Ana,Codée, Jeroen D. C.,Jiménez-Barbero, Jesús,Adamo, Roberto
, p. 16277 - 16287 (2019/11/14)
Group B Streptococcus serotypes Ia and Ib capsular polysaccharides are key targets for vaccine development. In spite of their immunospecifity these polysaccharides share high structural similarity. Both are composed of the same monosaccharide residues and
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.