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  • 1.
    Aisenbrey, Christopher
    et al.
    Institut de Chimie Universit0 Louis Pasteur Strasbourg—CNRS, UMR 7177 4, Rue Blaise Pascal, 67000 Strasbourg (France); Max-Planck-Institut f>r Biochemie Am Klopferspitz 18A, 82152 Martinsried (Germany).
    Cusan, Monica
    Lambotte, Stephan
    Jasperse, Pieter
    Georgescu, Julia
    Harzer, Ulrike
    Bechinger, Burkhard
    Specific Isotope Labeling of Colicin E1 and B Channel Domains For Membrane Topological Analysis by Oriented Solid-State NMR Spectroscopy2008Ingår i: ChemBioChem (Print), ISSN 1439-4227, E-ISSN 1439-7633, Vol. 9, nr 6, s. 944-951Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    An approach is presented to selectively label the methionines of the colicin E1 and B channel domains, each about 200 residues in size, and use them for oriented solid-state NMR investigations. By combining site-directed mutagenesis, bacterial overexpression in a methionine auxotroph E. coli strain and biochemical purification, quantitative amounts of the proteins for NMR structural investigations were obtained. The proteins were selectively labeled with 15N at only one, or at a few, selected sites. Multidimensional heteronuclear correlation high-resolution NMR spectroscopy and mass spectrometry were used to monitor the quality of isotopic labeling. Thereafter the proteins were reconstituted into oriented phospholipid bilayers and investigated by proton-decoupled 15N solid-state NMR spectroscopy. The colicin E1 thermolytic fragment that carries a single 15N methionine within its hydrophobic helix 9 region exhibited 15N resonances that are characteristic of helices that are oriented predominantly parallel to the membrane surface at low temperature, and a variety of alignments and conformations at room temperature. This suggests that the protein can adopt both umbrella and pen-knife conformations.

  • 2.
    Gröbner, Gerhard
    Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen.
    Lipids and Cellular Membranes in Amyloid Diseases: Edited by Raz Jelinek2011Ingår i: ChemBioChem (Print), ISSN 1439-4227, E-ISSN 1439-7633, Vol. 12, nr 17, s. 2699-2700Artikel, recension (Refereegranskat)
  • 3.
    Johansson, Susanne M C
    et al.
    Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen.
    Arnberg, Niklas
    Umeå universitet, Medicinska fakulteten, Institutionen för klinisk mikrobiologi, Virologi.
    Elofsson, Mikael
    Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen.
    Wadell, Göran
    Umeå universitet, Medicinska fakulteten, Institutionen för klinisk mikrobiologi, Virologi.
    Kihlberg, Jan
    Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen.
    Multivalent HSA conjugates of 3 '-siallyllactose are potent inhibitors of adenoviral cell attachment and infection2005Ingår i: ChemBioChem (Print), ISSN 1439-4227, E-ISSN 1439-7633, Vol. 6, nr 2, s. 358-364Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Adenoviruses of serotypes 8, 19 and 37 are the major cause of the severe eye infection EKC (epidemic keratoconjunctivitis). In general, all adenoviruses interact with their cellular receptors through the fibre proteins, which extend from the virus particle. Recently, adenovirus type 37 (Ad37) was found to bind and infect human corneal cells through attachment to carbohydrate structures that carry terminal alpha-(2-3)-linked sialic acids. Herein we present a synthetic route to a 3'-sialyllactose derivative and corresponding multivalent HSA conjugates with varying orders of valency. The potential of these compounds as inhibitors of EKC causing adenovirus of serotype Ad37, was studied with both binding assay and an infectivity assay. The results revealed that these compounds effectively prevent Ad37 from binding to and infecting human corneal epithelial (HCE) cells. Moreover, the inhibition is significantly increased with higher orders of multivalency.

  • 4. Kaspersen, Jørn D.
    et al.
    Pedersen, Jannik N.
    Hansted, Jon G.
    Nielsen, Søren B.
    Sakthivel, Srinivasan
    Wilhelm, Kristina
    Umeå universitet, Medicinska fakulteten, Institutionen för medicinsk kemi och biofysik.
    Nemashkalova, Ekaterina L.
    Permyakov, Sergei E.
    Permyakov, Eugene A.
    Pinto Oliveira, Cristiano Luis
    Morozova-Roche, Ludmilla A
    Umeå universitet, Medicinska fakulteten, Institutionen för medicinsk kemi och biofysik.
    Otzen, Daniel E.
    Pedersen, Jan Skov
    Generic structures of cytotoxic liprotides: nano-sized complexes with oleic acid cores and shells of disordered proteins2014Ingår i: ChemBioChem (Print), ISSN 1439-4227, E-ISSN 1439-7633, Vol. 15, nr 18, s. 2693-2702Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    The cytotoxic complex formed between alpha-lactalbumin and oleic acid (OA) has inspired many studies on protein-fatty acid complexes, but structural insight remains sparse. After having used small-angle X-ray scattering (SAXS) to obtain structural information, we present a new, generic structural model of cytotoxic protein-oleic acid complexes, which we have termed liprotides (lipids and partially denatured proteins). Twelve liprotides formed from seven structurally unrelated proteins and prepared by different procedures all displayed core-shell structures, each with a micellar OA core and a shell consisting of flexible, partially unfolded protein, which stabilizes the OA micelle. The common structure explains similar effects exerted on cells by different liprotides and is consistent with a cargo off-loading of the OA into cell membranes.

  • 5. Martinez, Nancy E.
    et al.
    Zimmermann, Tobias J.
    Goosmann, Christian
    Alexander, Tobias
    Hedberg, Christian
    Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen. Umeå universitet, Medicinska fakulteten, Umeå Centre for Microbial Research (UCMR).
    Ziegler, Slava
    Zychlinsky, Arturo
    Waldmann, Herbert
    Tetrahydroisoquinolines: New Inhibitors of Neutrophil Extracellular Trap (NET) Formation2017Ingår i: ChemBioChem (Print), ISSN 1439-4227, E-ISSN 1439-7633, Vol. 18, nr 10, s. 888-893Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Neutrophils are short-lived leukocytes that migrate to sites of infection as part of the acute immune response, where they phagocytose, degranulate, and form neutrophil extracellular traps (NETs). During NET formation, the nuclear lobules of neutrophils disappear and the chromatin expands and, accessorized with neutrophilic granule proteins, is expelled. NETs can be pathogenic in, for example, sepsis, cancer, and autoimmune and cardiovascular diseases. Therefore, the identification of inhibitors of NET formation is of great interest. Screening of a focused library of natural-product-inspired compounds by using a previously validated phenotypic NET assay identified a group of tetrahydroisoquinolines as new NET formation inhibitors. This compound class opens up new avenues for the study of cellular death through NET formation (NETosis) at different stages, and might inspire new medicinal chemistry programs aimed at NET-dependent diseases.

  • 6.
    Mogemark, Mickael
    et al.
    Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen.
    Elofsson, Mikael
    Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen.
    Kihlberg, Jan
    Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen.
    Fluorinated Protective Groups for On-Resin Quantification of Solid- Phase Oligosaccharide Synthesis with 19F NMR Spectroscopy2002Ingår i: ChemBioChem (Print), ISSN 1439-4227, E-ISSN 1439-7633, Vol. 3, nr 12, s. 1266-1269Artikel i tidskrift (Refereegranskat)
  • 7. Müller, Matthias P
    et al.
    Albers, Michael F
    Itzen, Aymelt
    Hedberg, Christian
    Exploring adenylylation and phosphocholination as post-translational modifications.2014Ingår i: ChemBioChem (Print), ISSN 1439-4227, E-ISSN 1439-7633, Vol. 15, nr 1Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Editing the translations: Adenylylation and phosphocholination have recently been found as important post-translational modifications used by pathogenic bacteria during the infection process. This review discusses the combined use of chemical handles and specific antibodies for the identification of previously unknown substrates of these post-translational modifications in infected host cells.

  • 8.
    Ochtrop, Philipp
    et al.
    Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen.
    Ernst, Stefan
    Itzen, Aymelt
    Hedberg, Christian
    Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen.
    Exploring the Substrate Scope of the Bacterial Phosphocholine Transferase AnkX for Versatile Protein Functionalization2019Ingår i: ChemBioChem (Print), ISSN 1439-4227, E-ISSN 1439-7633, Vol. 20, nr 18, s. 2336-2340Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Site-specific protein functionalization has become an indispensable tool in modern life sciences. Here, tag-based enzymatic protein functionalization techniques are among the most versatilely applicable approaches. However, many chemo-enzymatic functionalization strategies suffer from low substrate scopes of the enzymes utilized for functional labeling probes. We report on the wide substrate scope of the bacterial enzyme AnkX towards derivatized CDP-choline analogues and demonstrate that AnkX-catalyzed phosphocholination can be used for site-specific one- and two-step protein labeling with a broad array of different functionalities, displaying fast second-order transfer rates of 5x10(2) to 1.8x10(4) m(-1) s(-1). Furthermore, we also present a strategy for the site-specific dual labeling of proteins of interest, based on the exploitation of AnkX and the delabeling function of the enzyme Lem3. Our results contribute to the wide field of protein functionalization, offering an attractive chemo-enzymatic tag-based modification strategy for in vitro labeling.

  • 9.
    Svensson, Anette
    et al.
    Organic Chemistry 2 Center for Chemistry and Chemical Engineering Lund Institute of Technology, Lund University P.O. Box 124, SE-221 00 Lund, Sweden.
    Larsson, Andreas
    Umeå universitet, Teknisk-naturvetenskaplig fakultet, Kemi.
    Emtenäs, Hans
    Umeå universitet, Teknisk-naturvetenskaplig fakultet, Kemi.
    Hedenström, Mattias
    Umeå universitet, Teknisk-naturvetenskaplig fakultet, Kemi.
    Fex, Tomas
    3Active Biotech, Lund Research Center P.O. Box 724, SE-220 07 Lund, Sweden.
    Hultgren, Scott J.
    Department of Molecular Microbiology Washington University School of Medicine 660 South Euclid Avenue, St. Louis, MO 63110, USA.
    Pinker, Jerome S.
    Department of Molecular Microbiology Washington University School of Medicine 660 South Euclid Avenue, St. Louis, MO 63110, USA.
    Almqvist, Fredrik
    Umeå universitet, Teknisk-naturvetenskaplig fakultet, Kemi.
    Kihlberg, Jan
    Umeå universitet, Teknisk-naturvetenskaplig fakultet, Kemi.
    Design and evaluation of Pilicides: Potential novel antibacterial agents directed against Uropathogenic Escherichia coli2001Ingår i: ChemBioChem (Print), ISSN 1439-4227, E-ISSN 1439-7633, ChemBioChem (Online), ISSN '1439-7633', Vol. 2, nr 12, s. 915-918Artikel i tidskrift (Refereegranskat)
  • 10.
    Wallner, Fredrik K.
    et al.
    Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen.
    Chen, Liying
    Moliner, Annalena
    Jondal, Mikael
    Elofsson, Mikael
    Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen.
    Loading of the antigen-presenting protein CD1d with synthetic glycolipids2004Ingår i: ChemBioChem (Print), ISSN 1439-4227, E-ISSN 1439-7633, Vol. 5, nr 4, s. 437-444Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    CD1 proteins present mammalian and microbial lipid and glycolipid antigens to different subsets of T cells. Few such antigens have been identified and the binding of these to CD1 molecules has mainly been studied by using responding T cells in cellular assays or recombinant solid-phase CD1 proteins. In the present study we use four different glycolipids, some of which contain tumor-associated carbohydrate antigens, to develop a procedure to easily detect binding of glycolipids to CD1 proteins on viable cells. Two of these glycolipids are novel glycoconjugates containing -D-N-acetylgalactosamine (-GalNAc) that were prepared by a combined solution and solid-phase approach. The key step, a Fischer glycosylation of 9-fluorenylmethoxycarbonylaminoethanol with GalNAc, furnished the -glycoside 4 in 34 % yield. Cells were incubated with glycolipids and stained with monoclonal antibodies specific for the carbohydrate part. The level of glycolipid bound to cells was then determined by flow cytometry with a secondary antibody labeled with fluorescein isothiocyanate. All four glycolipids were found to bind to CD1d but with different selectivity. The loading was dose dependent and could be inhibited by an established CD1d ligand, -galactosylceramide. Through use of this procedure, glycolipids were selectively loaded onto CD1d expressed on professional antigen-presenting cells for future use as cellular vaccines. Moreover, the glycolipids described in this study represent novel CD1d-binding ligands that will be useful derivatives in the study of CD1d-dependent immune responses, for example, against tumors.

  • 11.
    Wellner, Eric
    et al.
    Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen.
    Gustafsson, Tomas
    Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen.
    Bäcklund, Johan
    Holmdahl, Rikard
    Kihlberg, Jan
    Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen.
    Synthesis of a C-glycoside analogue of β-D-galactosyl hydroxynorvaline and its use in immunological studies2000Ingår i: ChemBioChem (Print), ISSN 1439-4227, E-ISSN 1439-7633, Vol. 1, nr 4, s. 272-280Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    A C-linked isostere of β-d-galactosylated hydroxynorvaline has been prepared in eight steps from per-O-benzylated galactopyranolactone. Addition of a homoallylic Grignard reagent to the lactone, reduction of the resulting hemiacetal with triethylsilane, and a Wittig reaction with Garner's aldehyde were key steps in this synthesis. The C-linked building block was then incorporated at position 264 into the fragment CII(256–270) from type II collagen by solid-phase synthesis using a combination of the tert-butoxycarbonyl (Boc) and 9-fluorenylmethoxycarbonyl (Fmoc) protective group strategies. Deprotection of the benzylated C-linked galactosyl moiety was achieved simultaneously with cleavage of the glycopeptide from the solid phase by using triethylsilyl trifluoromethanesulfonate in TFA. Helper T-cell hybridomas obtained in a mouse model for rheumatoid arthritis responded to the C-linked glycopeptide when presented by class II MHC molecules. However, 10- to 20-fold higher concentrations were required as compared to when O-linked β-d-galactosylated hydroxynorvaline or hydroxylysine (Hyl) were present at position 264 of CII(256–270). Thus, replacement of a single oxygen atom by a methylene group in the carbohydrate moiety of a glycopeptide antigen had a substantial influence on the T-cell response. This reveals that T cells are able to recognize the carbohydrate moiety of glycopeptide antigens with high specificity. Finally, the results suggest that structural modifications of β-d-Gal-Hyl264in CII(256–270) may give altered peptide ligands that can be used for induction of tolerance in autoimmune rheumatoid arthritis.

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