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  • 1.
    Aldén, Anna
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Påhlsson, Peter
    Rydén, I
    HPLC analysis of carbohydrate deficient transferrin isoforms isolated by the Axis-Shield %CDT method2005In: Clinica chimica acta, Vol. 356 (1-2), p. 143-146Article in journal (Refereed)
  • 2. Aldén, Anna
    et al.
    Persson, Anna
    Christensson, Kerstin
    Holmqvist, Olov
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Porcine platelet lysate as a supplement for animal cell culture2007In: Cytotechnology (Dordrecht), ISSN 0920-9069, E-ISSN 1573-0778, Vol. 55, p. 3-8Article in journal (Refereed)
  • 3.
    Andersson, Håkan S.
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Koch-Schmidt, Ann-Christin
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Study of the Nature of Recognition in Molecularly Imprinted Polymers1996In: J. Mol. Recogn., Vol. 9, p 675-682Article in journal (Refereed)
  • 4.
    Andersson, Håkan S.
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Koch-Schmidt, Ann-Christin
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Mosbach, Klaus
    Lund University.
    Study of Weak Affinity Interactions in Molecularly Imprinted Polymers1995In: Journal of Molecular Recognition, ISSN 0952-3499, E-ISSN 1099-1352, Vol. 8, no 3, p. 231-Article in journal (Other academic)
  • 5.
    Bergström, Maria
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Liu, Shuang
    Kiick, Kristi
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Cholera toxin inhibitors studied with High-performance liquid affinity chromatography: arobust method to evaluate receptor-ligand interactions2009In: Chemical Biology and Drug Design, ISSN 1747-0277, E-ISSN 1747-0285, Vol. 73, no 1, p. 132-141Article in journal (Refereed)
    Abstract [en]

    Anti-adhesion drugs may be an alternative to antibiotics to control infection of micro-organisms. The well-characterized interaction between cholera toxin and the cellular glycolipid GM1 makes it an attractive model for inhibition studies in general. In this report, we demonstrate a high-performance liquid affinity chromatography approach called weak affinity chromatography to evaluate cholera toxin inhibitors. The cholera toxin B-subunit was covalently coupled to porous silica and a (weak) affinity column was produced. The K(D) values of galactose and meta-nitrophenyl alpha-d-galactoside were determined with weak affinity chromatography to be 52 and 1 mm, respectively, which agree well with IC(50) values previously reported. To increase inhibition potency multivalent inhibitors have been developed and the interaction with multivalent glycopolypeptides was also evaluated. The affinity of these compounds was found to correlate with the galactoside content but K(D) values were not obtained because of the inhomogeneous response and slow off-rate from multivalent interactions. Despite the limitations in obtaining direct K(D) values of the multivalent galactopolypeptides, weak affinity chromatography represents an additional and valuable tool in the evaluation of monovalent as well as multivalent cholera toxin inhibitors. It offers multiple advantages, such as a low sample consumption, high reproducibility and short analysis time, which are often not observed in other methods of analysis.

  • 6.
    Bergström, Maria
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Lundblad, Arne
    Påhlsson, Peter
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Use of weak monoclonal antibodies for affinity chromatography1998In: Journal of Molecular Recognition, Vol. 11, p. 110-113Article in journal (Refereed)
  • 7.
    Bergström, Maria
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Nilsson, Mikael
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Isaksson, Roland
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Rydén, I
    Påhlsson, Peter
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Lectin Affinity Capillary Electrophoresis in Glycoform Analysis Applying the Partial Filling Technique2004In: Journal of Chromatography B, Vol. 809, p. 323-329Article in journal (Refereed)
  • 8.
    Bergström, Maria
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Use of perfusive supports in weak affinity chromatography (WAC)2001In: Bio-chromatography, Vol. 6, p. 163-172Article in journal (Refereed)
  • 9.
    Bergström, Maria
    et al.
    Linnaeus University, Faculty of Science and Engineering, School of Natural Sciences.
    Åström, Eva
    Påhlsson, Peter
    Ohlson, Sten
    Linnaeus University, Faculty of Science and Engineering, School of Natural Sciences.
    Elucidating the selectivity of recombinant forms of Aleuria aurantia lectin using weak affinity chromatography2012In: Journal of chromatography. B, ISSN 1570-0232, E-ISSN 1873-376X, Vol. 885-886, p. 66-72Article in journal (Refereed)
    Abstract [en]

    Aberrant glycosylation is connected to several pathological conditions and lectins are useful tools to characterize glycosylated biomarkers. The Aleuria aurantia lectin (AAL) is of special interest since it interacts with all types of fucosylated saccharides. AAL has been expressed in E.coli as a fully functional recombinant protein. Engineered variants of AAL have been developed with the aim of creating monovalent lectins with more homogenous binding characteristics. Four different forms of AAL were studied in the present work: native AAL purified from Aleuria aurantia mushrooms, recombinant AAL dimer, recombinant AAL monomer and recombinant AAL site 2 (S2-AAL). The affinities of these AAL forms towards a number of saccharides were determined with weak affinity chromatography (WAC). Disaccharides with fucose linked α1-3 to GlcNAc interacted with higher affinity compared to fucose linked α1-6 or α1-4 and the obtained dissociation constants (Kd) were in the range of 10 μM for all AAL forms. Tetra- and pentasaccharides with fucose in α1-2, α1-3 or α1-4 had Kd values ranging from 0.1–7 mM while a large α1-6 fucosylated oligosaccharide had a Kd of about 20 μM. The recombinant multivalent AAL forms and native AAL exhibited similar affinities towards all saccharides, but S2-AAL had a lower affinity especially regarding a sialic acid containing fucosylated saccharide. It was demonstrated that WAC is a valuable technique in determining the detailed binding profile of the lectins. Specific advantages with WAC include a low consumption of non-labeled saccharides, possibility to analyze mixtures and a simple procedure using standard HPLC equipment.

  • 10. Bratt, T
    et al.
    Ohlson, Sten
    Perstorp Biolytica AB, S-223 70 Lund, Sweden.
    The Development of a C1q ANTI-C1q Immunoadsorbent for Removal of Immune Complexes from Plasma1988In: Journal of Clinical Laboratory Immunology, ISSN 0141-2760, Vol. 27, p. 191-195Article in journal (Refereed)
    Abstract [en]

    An immunoadsorbent based on immobilized C1q has been developed to remove possibly pathogenic immune complexes from plasma deriving from patients suffering from systemic lupus erythematosus or rheumatoid arthritis. Traditional immobilization procedures based on, e.g., cyanogen bromide activation could not be used to produce an efficient adsorbent. However, by using antibodies directed towards C1q as handles for the immobilization of C1q it was possible to make an adsorbent that efficiently bound immune complexes in plasma. The capacity of the C1q anti-C1q adsorbent to bind artificial immune complexes such as aggregated human globulins or immune complexes from various plasma samples was evaluated. Both batch and column experiments were conducted. The typical capacity in batch was about 1 mg immune complexes/ml gel when incubated with patient plasma samples with high titers of immune complexes. Special attention has to be paid to leakage of undesirable components from the adsorbent. It was found that leakage of C1q occurred but it was not more than after covalent immobilization procedures such as cyanogen bromide. 

  • 11. Bratt, T
    et al.
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Borregaard, N
    Interactions between neutrophil gelatinase-associated lipocalin and natural hydrophobic ligands1999In: Biochimica et biophysica acta, Vol. 1472, p. 262-266Article in journal (Refereed)
  • 12.
    Duong-Thi, Minh-Dao
    et al.
    Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences.
    Bergström, Gunnar
    Linköping Univ, Sweden.
    Mandenius, Carl-Fredrik
    Linköping Univ, Sweden.
    Bergström, Maria
    Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences.
    Fex, Tomas
    Univ Gothenburg, Sweden.
    Ohlson, Sten
    Nanyang Technol Univ, Singapore.
    Comparison of weak affinity chromatography and surface plasmon resonance in determining affinity of small molecules2014In: Analytical Biochemistry, ISSN 0003-2697, E-ISSN 1096-0309, Vol. 461, p. 57-59Article in journal (Refereed)
    Abstract [en]

    In this study, we compared affinity data from surface plasmon resonance (SPR) and weak affinity chromatography (WAC), two established techniques for determination of weak affinity (mM-mu M) small molecule-protein interactions. In the current comparison, thrombin was used as target protein. In WAC the affinity constant (K-D) was determined from retention times, and in SPR it was determined by Langmuir isotherm fitting of steady-state responses. Results indicate a strong correlation between the two methods (R-2 = 0.995, P < 0.0001). (C) 2014 Elsevier Inc. All rights reserved.

  • 13.
    Duong-Thi, Minh-Dao
    et al.
    Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences. Nanyang Technol University, Singapore.
    Bergström, Maria
    Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences.
    Edwards, Katarina
    Uppsala University.
    Eriksson, Jonny
    Uppsala University.
    Ohlson, Sten
    Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences.
    To Yiu Ying, Janet
    Nanyang Technol University, Singapore.
    Torres, Jaume
    Nanyang Technol University, Singapore.
    Agmo Hernández, Víctor
    Uppsala University.
    Lipodisks integrated with weak affinity chromatography enable fragment screening of integral membrane proteins2016In: The Analyst, ISSN 0003-2654, E-ISSN 1364-5528, Vol. 141, no 3, p. 981-988Article in journal (Refereed)
    Abstract [en]

    Membrane proteins constitute the largest class of drug targets but they present many challenges in drug discovery. Importantly, the discovery of potential drug candidates is hampered by the limited availability of efficient methods for screening drug-protein interactions. In this work we present a novel strategy for rapid identification of molecules capable of binding to a selected membrane protein. An integral membrane protein (human aquaporin-1) was incorporated into planar lipid bilayer disks (lipodisks), which were subsequently covalently coupled to porous derivatized silica and packed into HPLC columns. The obtained affinity columns were used in a typical protocol for fragment screening by weak affinity chromatography (WAC), in which one hit was identified out of a 200 compound collection. The lipodisk-based strategy, which ensures a stable and native-like lipid environment for the protein, is expected to work also with other membrane proteins and screening procedures.

  • 14.
    Duong-Thi, Minh-Dao
    et al.
    Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences.
    Bergström, Maria
    Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences.
    Fex, Tomas
    Astra& Zeneca R&D Mölndal, Mölndal, Sweden.
    Isaksson, Roland
    Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences.
    Ohlson, Sten
    Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences.
    High-Throughput Fragment Screening by Affinity LC-MS2013In: Journal of Biomolecular Screening, ISSN 1087-0571, E-ISSN 1552-454X, Vol. 18, no 2, p. 160-171Article in journal (Refereed)
    Abstract [en]

    Fragment screening, an emerging approach for hit finding in drug discovery, has recently been proven effective by its first approved drug, vemurafenib, for cancer treatment. Techniques such as nuclear magnetic resonance, surface plasmon resonance, and isothemal titration calorimetry, with their own pros and cons, have been employed for screening fragment libraries. As an alternative approach, screening based on high-performance liquid chromatography separation has been developed. In this work, we present weak affinity LC/MS as a method to screen fragments under high-throughput conditions. Affinity-based capillary columns with immobilized thrombin were used to screen a collection of 590 compounds from a fragment library. The collection was divided into 11 mixtures (each containing 35 to 65 fragments) and screened by MS detection. The primary screening was performed in < 4 h (corresponding to > 3500 fragments per day). Thirty hits were defined, which subsequently entered a secondary screening using an active site-blocked thrombin column for confirmation of specificity. One hit showed selective binding to thrombin with an estimated dissociation constant (K-D) in the 0.1 mM range. This study shows that affinity LC/MS is characterized by high throughput, ease of operation, and low consumption of target and fragments, and therefore it promises to be a valuable method for fragment screening.

  • 15.
    Duong-Thi, Minh-Dao
    et al.
    Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences.
    Bergström, Maria
    Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences.
    Fex, Tomas
    Astra&Zeneca R&D, Sweden.
    Svensson, Susanne
    Chalmers University of Technology, Sweden.
    Ohlson, Sten
    Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences.
    Isaksson, Roland
    Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences.
    Weak Affinity Chromatography for Evaluation of Stereoisomers in Early Drug Discovery2013In: Journal of Biomolecular Screening, ISSN 1087-0571, E-ISSN 1552-454X, Vol. 18, no 6, p. 748-755Article in journal (Refereed)
    Abstract [en]

    In early drug discovery (e.g. in fragment screening), recognition of stereoisomeric structures is valuable and guides medicinal chemists to focus only on useful configurations. In this work, we concurrently screened mixtures of stereoisomers and estimated their affinities to a protein target (thrombin) using weak affinity chromatography-mass spectrometry (WAC-MS). Affinity determinations by WAC showed that minor changes in stereoisomeric configuration could have major impact on affinity. The ability of WAC-MS to provide instant information about stereoselectivity and binding affinities directly from analyte mixtures is a great advantage in fragment library screening and drug lead development.

  • 16.
    Duong-Thi, Minh-Dao
    et al.
    Linnaeus University, Faculty of Science and Engineering, School of Natural Sciences.
    Meiby, Elinor
    Linnaeus University, Faculty of Science and Engineering, School of Natural Sciences.
    Bergström, Maria
    Linnaeus University, Faculty of Science and Engineering, School of Natural Sciences.
    Fex, Tomas
    Isaksson, Roland
    Linnaeus University, Faculty of Science and Engineering, School of Natural Sciences.
    Ohlson, Sten
    Linnaeus University, Faculty of Science and Engineering, School of Natural Sciences.
    Weak affinity chromatography as a new approach for fragment screening in drug discovery2011In: Analytical Biochemistry, ISSN 0003-2697, E-ISSN 1096-0309, Vol. 414, no 1, p. 138-146Article in journal (Refereed)
    Abstract [en]

    Fragment-based drug design (FBDD) is currently being implemented in drug discovery, creating a demand for developing efficient techniques for fragment screening. Due to the intrinsic weak or transient binding of fragments (mM–uM in dissociation constant (KD)) to targets, methods must be sensitive enough to accurately detect and quantify an interaction. This study presents weak affinity chromatography (WAC) as an alternative tool for screening of small fragments. The technology was demonstrated by screening of a selected 23 compound fragment collection of documented binders, mostly amidines, using trypsin and thrombin as model target protease proteins. WAC was proven to be a sensitive, robust, and reproducible technique that also provides information about affinity of a fragment in the range of 1 mM–10uM. Furthermore, it has potential for high throughput as was evidenced by analyzing mixtures in the range of 10 substances by WAC–MS. The accessibility and flexibility of the technology were shown as fragment screening can be performed on standard HPLC equipment. The technology can further be miniaturized and adapted to the requirements of affinity ranges of the fragment library. All these features of WAC make it a potential method in drug discovery for fragment screening.

  • 17.
    Engström, Henrik
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Andersson, Per Ola
    Gregorius, Klaus
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Towards a FRET-based immunosensor for continuous carbohydrate monitoring2008In: JIM - Journal of Immunological Methods, ISSN 0022-1759, E-ISSN 1872-7905, Vol. 333, no 1-2, p. 107-114Article in journal (Refereed)
    Abstract [en]

    In this report we have evaluated the potential of using fluorescence/Förster resonance energy transfer (FRET) in a competitive immunosensor for continuous monitoring of the carbohydrate hapten maltose. The cyanine dyes Cy5 and Cy5.5 were used as a donor–acceptor pair by conjugation to maltose-labeled bovine serum albumin (BSA) and the monoclonal antibody IgG 39.5, giving Cy5–BSA–maltotriitol (3.1/1/18) and Cy5.5–mAb39.5 (2.2/1), respectively. This antibody with weak affinity towards maltose showed full reversibility to both the free maltose and the maltose-labeled conjugate. It allowed us to measure continuously the maltose content by monitoring the FRET signal change over time due to displacement of Cy5–BSA–maltotriitol from Cy5.5–mAb39.5 inside a semipermeable capsule. A near 22% total increase was seen in the fluorescence intensity ratio I670/I700 in the presence of maltose, with a calculated EC50 = 1.87 ± 0.13 mM (R2 = 0.9984) from the sigmoidal dose–response curve at 25 °C. Specificity of the immunosensor was shown with the structural analog to maltose, cellobiose, and it generated no detectable response. A minor drift in the sensor baseline was seen with 0.4% per 24 h, which was in the same magnitude as the signal-to-noise ratio, during the 4 weeks of measurements. The immunosensor was applied to crude samples of oat drinks for direct quantification of the maltose content. Overall, this work demonstrates the potential to use an immunosensor based on weakly binding antibodies and FRET technology for remote and non-invasive carbohydrate monitoring.

  • 18.
    Engström, Henrik
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Andersson, Per Ola
    Ohlson, Sten
    A label-free continuous total-internal-reflection-flourescence-based immunosensor2006In: Analytical Biochemistry, ISSN 0003-2697, Vol. 357, no 2, p. 159-166Article in journal (Refereed)
  • 19.
    Engström, Henrik
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Andersson, Per Ola
    Ohlson, Sten
    Analysis of the specificity and thermodynamics of the interaction betwwen low affinity antibodies and carbohydrate antigens using flourescence spectroscopy2005In: Journal of Immunological Methods, ISSN 0022-1759, Vol. 297, no 1, p. 203-211Article in journal (Refereed)
  • 20.
    Engström, Henrik
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Johansson, Reine
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Koch-Schmidt, Per
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Gregorius, Klaus
    PreciSense A/S, Dr Neergaards Vej 3, DK-2970 Hørsholm, Denmark.
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Bergström, Maria
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Evaluation of a glucose sensing antibody using weak affinity chromatography2008In: BMC Biomedical chromotography, ISSN 0269-3879, E-ISSN 1099-0801, Vol. 22, no 3, p. 272-277Article in journal (Refereed)
    Abstract [en]

    Continuous monitoring of drug levels and endogenous molecules in biological fluids is a developing research area with many applications. One example is the need to improve life for millions of diabetes mellitus patients by continuously monitoring the glucose level. In order to have a dynamic response, the recognition molecule in a continuous sensor should preferentially have a fast dissociation rate and a dissociation constant in the millimolar range. We have evaluated the monoclonal antibody (mAb) 3F1E8-A2 for its potential to be used in a future glucose sensor application. The mAb was generated from hybridomas by immunizing mice with 10 kDa dextran (an α1,6-glucose polymer) with the aim of obtaining mAbs that can recognize the glucose monomer. The mAb was immobilized to macroporous silica and the interaction with dextran-derived oligosaccharides was evaluated with weak affinity chromatography (WAC). To measure the low affinities between the mAb 3F1E8-A2 and different monosaccharides, a competitive weak affinity chromatography approach was employed. It was found that the mAb had a higher specificity for glucose compared with other monosaccharides and the dissociation constant (Kd) towards glucose was determined as 18.8 ± 2.6 mm.

  • 21.
    Engström, Henrik
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Gene Stubbs, E.
    Maciulis, Alma
    Caldwell, Virgil
    Dennis Odell, J.
    R. Torres, Anthony
    Decreased Expression of CD95 (FAS/APO-1) on CD4+ T-lymphocytes from Participants with Autism2003In: Journal of Developmental and Physical Disabilities, Vol. 15, p. 155-163Article in journal (Refereed)
  • 22. Freiburghaus, C
    et al.
    Ohlson, Sten
    Perstorp Biolytica AB, S-223 70 Lund, Sweden.
    Nilsson, I M
    Extracorporeal Systems for Adsorption of Antibodies in Hemophilia A and B1988In: Methods in Enzymology, ISSN 0076-6879, E-ISSN 1557-7988, Vol. 137, p. 458-466Article in journal (Refereed)
  • 23. Glad, M
    et al.
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Hansson, L
    Månsson, M O
    Larsson, P O
    Mosbach, K
    Separation Agent1983Patent (Other (popular science, discussion, etc.))
  • 24. Glad, M
    et al.
    Ohlson, Sten
    Dep. Pure and Applied Biochemistry, Chemical Center, University of Lund, P.O. Box 740, S-220 07 Lund 7, Sweden.
    Hansson, L
    Månsson, M O
    Mosbach, K
    High-Performance Liquid Affinity Chromatography of Nucleosides, Nucleotides and Carbonhydrates with Boronic Acid-Substituted Microparticulate Silica1980In: Journal of Chromatography, Vol. 200, p. 254-260Article in journal (Refereed)
  • 25.
    Johansson, Liselotte
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Klinth, Jeanna
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Holmqvist, O
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Platelet Lysate: A Replacement for Fetal Bovine Serum in Animal Cell Culture2003In: Cytotechnology, Vol. 42, p. 67-74Article in journal (Refereed)
  • 26.
    Johansson, Reine
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Gunnarsson, L C
    Ohlin, M
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Thermostable carbohydrate-binding modules in affinity chromatography2006In: Journal of molecular recognition, Vol. 19, no 4, p. 275-281Article in journal (Refereed)
  • 27.
    Johansson, Reine
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Ohlin, M
    Jansson, B
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Transiently binding antibody fragments against Lewis x and sialyl-Lewis x2006In: Journal of immunological methods, Vol. 312, no 1-2, p. 20-26Article in journal (Refereed)
  • 28.
    Johansson, Susanne
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Polacek, Charlotta
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Nilsson, Anne
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Lindberg, A. Michael
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Studies of weak-to-moderate virus-receptor interactions using uncloned viruses as well as an infectious cDNA clone of echovirus 7 strain Wallace1996Conference paper (Refereed)
  • 29. Jungar, C
    et al.
    Strandh, Magnus
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Mandenius, C-F
    Analysis of Carbohydrates using Liquid Chromatography - Surface Plasmon Resonance Immunosensing Systems2000In: Analytical biochemistry, Vol. 281, p. 151-158Article in journal (Refereed)
  • 30.
    Landström, Jens
    et al.
    Stockholm Univ, Dept Organ Chem, Arrhenius Lab, S-10691 Stockholm.
    Bergström, Maria
    Linnaeus University, Faculty of Science and Engineering, School of Natural Sciences.
    Hamark, Christoffer
    Stockholm Univ, Dept Organ Chem, Arrhenius Lab, S-10691 Stockholm.
    Ohlson, Sten
    Linnaeus University, Faculty of Science and Engineering, School of Natural Sciences.
    Widmalm, Göran
    Stockholm Univ, Dept Organ Chem, Arrhenius Lab, S-10691 Stockholm.
    Combining weak affinity chromatography, NMR spectroscopy and molecular simulations in carbohydrate-lysozyme interaction studies.2012In: Organic and biomolecular chemistry, ISSN 1477-0520, E-ISSN 1477-0539, Vol. 10, no 15, p. 3019-3032Article in journal (Refereed)
    Abstract [en]

    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 (1)H saturation transfer difference (STD) effects and transferred (1)H,(1)H-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 (1)H 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.

  • 31. Larsson, P O
    et al.
    Glad, M
    Hansson, L
    Månsson, M O
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Mosbach, K
    High-Performance Liquid Affinity Chromatography1983In: Advances in chromatography: Vol. 21 / [ed] J Calvin Giddings, New York, Basel: Marcel Dekker , 1983, p. 41-85Chapter in book (Other academic)
  • 32. Larsson, P O
    et al.
    Mosbach, K
    Ohlson, Sten
    Dep. Pure and Applied Biochemistry, Chemical Center, University of Lund, P.O. Box 740, S-220 07 Lund 7, Sweden.
    Antibiotic and Steriod Transformation Process1981Patent (Other (popular science, discussion, etc.))
  • 33. Larsson, P O
    et al.
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Mosbach, K
    New Approach to Steroid Conversion Using Immobilised Microorganisms1976In: Nature, Vol. 263, no 5580, p. 796-797Article in journal (Refereed)
    Abstract [en]

    The marked increase in demand for contraceptives and anti-inflammatory agents such as cortisol and prednisolone, combined with a diminishing supply of steroid raw materials may lead to shortages of steroid drugs1. Thus it is important to develop new sources for steroids as well as to devise more efficient means for steroid conversions. Here we report a new approach to steroid transformation in which activated immobilised microorganisms are utilised and which represents a promising alternative to conventional microbial transformation processes.

  • 34. Larsson, P O
    et al.
    Ohlson, Sten
    Dep. Pure and Applied Biochemistry, Chemical Center, University of Lund, P.O. Box 740, S-220 07 Lund 7, Sweden.
    Mosbach, K
    Steroid Conversion Using Immobilized Living Microorganisms1978In: Enzyme Engineering: Vol. 4 / [ed] G.H. Broun, G. Manecke and L.B. Wingard, Jr., New York: Plenum Publishing Corporation , 1978, p. 317-322Chapter in book (Other academic)
  • 35. Larsson, P O
    et al.
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Mosbach, K
    Transformation of Steroids by Immobilized Living Microorganisms1979In: Applied Biochemistry and Bioengineering, Vol. 2, p. 291-301Article in journal (Refereed)
  • 36. Leickt, Lisa
    et al.
    Bergström, Maria
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Zopf, David
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Bioaffinity chromatography in the 10 mM range of Kd1997In: Analytical biochemistry, Vol. 253, p. 135-136Article in journal (Refereed)
  • 37. Leickt, Lisa
    et al.
    Grubb, A
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Affinity Screening for Weak Monoclonal Antibodies1998In: Journal of immunological methods, Vol. 220 (1-2), p. 19-23Article in journal (Refereed)
  • 38. Leickt, Lisa
    et al.
    Grubb, A
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Development of Monoclonal Antibodies against creatine kinase CKMB22002In: Scandinavian journal of clinical and laboratory investigation, Vol. 62, p. 423-430Article in journal (Refereed)
  • 39. Leickt, Lisa
    et al.
    Grubb, A
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Screening for Weak Monoclonal Antibodies in Hybridoma Technology1998In: Journal of Molecular Recognition, Vol. 11, p. 114-117Article in journal (Refereed)
  • 40. Leickt, Lisa
    et al.
    Månsson, Alf
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Prediction of affinity and kinetics in biomolecular interaction by affinity chromatography2001In: Analytical Biochemistry, Vol. 291, p. 102-108Article in journal (Refereed)
  • 41. Liljeblad, M
    et al.
    Lundblad, Arne
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Påhlsson, Peter
    Detection of low Molecular Weight Heparin Oligossacharides (FRAGMIN) Using Surface Plasmon Resonance1998In: Journal of Molecular Recognition, Vol. 11, p. 191-194Article in journal (Refereed)
  • 42. Liljeblad, M
    et al.
    Rydén, I
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Lundblad, Arne
    Påhlsson, Peter
    A lectin immunosensor technique for determination of alfa1-acid glycoprotein fucosylation2001In: Analytical biochemistry, Vol. 288, p. 216-224Article in journal (Refereed)
  • 43. Ljungberg, H
    et al.
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Nilsson, S
    Exploitation of a Monoclonal Antibody for Weak Affinity Based Separation in Capillary Gel Electrophoresis1998In: Electrophoresis, Vol. 19, p. 461-464Article in journal (Refereed)
  • 44. Lowe, C R
    et al.
    Glad, M
    Larsson, P O
    Ohlson, Sten
    Dep. Pure and Applied Biochemistry, Chemical Center, University of Lund, P.O. Box 740, S-220 07 Lund 7, Sweden.
    Small, D A P
    Atkinson, Tony
    Mosbach, K
    High-Performance Liquid Affinity Chromatography of Proteins on Cibacron Blue F3G-A Bonded Silica1981In: Journal of Chromatography, Vol. 215, p. 303-316Article in journal (Refereed)
  • 45. Mandenius, Carl-Fredrik
    et al.
    Wang, Ronghui
    Aldén, Anna
    Bergström, Gunnar
    Thebault, Sabine
    Lutsch, Charles
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Monitoring of influenza virus hemagglutinin in process samples using weak affinity ligands and surface plasmon resonance2008In: Analytica Chimica Acta, ISSN 0003-2670, E-ISSN 1873-4324, Vol. 623, p. 66-75Article in journal (Refereed)
  • 46. Mattiasson, B
    et al.
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Affinity Interactions1998In: Journal of Molecular Recognition, Vol. 11Article in journal (Refereed)
  • 47.
    Meiby, Elinor
    et al.
    Linnaeus University, Faculty of Science and Engineering, School of Natural Sciences.
    Knapp, Stefan
    Elkins, Jonathan M.
    Ohlson, Sten
    Linnaeus University, Faculty of Science and Engineering, School of Natural Sciences.
    Fragment screening of cyclin G-associated kinase by weak affinity chromatography2012In: Analytical and Bioanalytical Chemistry, ISSN 1618-2642, E-ISSN 1618-2650, Vol. 404, no 8, p. 2417-2425Article in journal (Refereed)
    Abstract [en]

    Fragment-based drug discovery (FBDD) has become a new strategy for drug discovery where lead compounds are evolved from small molecules. These fragments form low affinity interactions (dissociation constant (K (D)) = mM -aEuro parts per thousand mu M) with protein targets, which require fragment screening methods of sufficient sensitivity. Weak affinity chromatography (WAC) is a promising new technology for fragment screening based on selective retention of fragments by a drug target. Kinases are a major pharmaceutical target, and FBDD has been successfully applied to several of these targets. In this work, we have demonstrated the potential to use WAC in combination with mass spectrometry (MS) detection for fragment screening of a kinase target-cyclin G-associated kinase (GAK). One hundred seventy fragments were selected for WAC screening by virtual screening of a commercial fragment library against the ATP-binding site of five different proteins. GAK protein was immobilized on a capillary HPLC column, and compound binding was characterized by frontal affinity chromatography. Compounds were screened in sets of 13 or 14, in combination with MS detection for enhanced throughput. Seventy-eight fragments (46 %) with K (D) < 200 mu M were detected, including a few highly efficient GAK binders (K (D) of 2 mu M; ligand efficiency = 0.51). Of special interest is that chiral screening by WAC may be possible, as two stereoisomeric fragments, which both contained one chiral center, demonstrated twin peaks. This ability, in combination with the robustness, sensitivity, and simplicity of WAC makes it a new method for fragment screening of considerable potential.

  • 48.
    Meiby, Elinor
    et al.
    Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences.
    M Zetterberg, Malin
    Uppsala University.
    Victor, Hernàndez
    Uppsala University.
    Ohlson, Sten
    Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences. Nanyang Technol Univ, Sch Biol Sci, Singapore 637551, Singapore.
    Edwards, Katarina
    Uppsala University.
    Immobilized lipodisks as model membranes in high-throughput HPLC-MS analysis.2013In: Analytical and Bioanalytical Chemistry, ISSN 1618-2642, E-ISSN 1618-2650, Vol. 405, no 14, p. 4859-4869Article in journal (Refereed)
    Abstract [en]

    Lipodisks, also referred to as polyethylene glycol (PEG)-stabilized bilayer disks, have previously been demonstrated to hold great potential as model membranes in drug partition studies. In this study, an HPLC-MS system with stably immobilized lipodisks is presented. Functionalized lipodisks were immobilized on two different HPLC support materials either covalently by reductive amination or by streptavidin-biotin binding. An analytical HPLC column with immobilized lipodisks was evaluated by analysis of mixtures containing 15 different drug compounds. The efficiency, reproducibility, and stability of the system were found to be excellent. In situ incorporation of cyclooxygenase-1 (COX-1) in immobilized lipodisks on a column was also achieved. Specific binding of COX-1 to the immobilized lipodisks was validated by interaction studies with QCM-D. These results, taken together, open up the possibility of studying ligand interactions with membrane proteins by weak affinity chromatography.

  • 49.
    Meiby, Elinor
    et al.
    Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences.
    Simmonite, Heather
    le Strat, Loic
    Davis, Ben
    Matassova, Natalia
    Moore, Jonathan D.
    Mrosek, Michael
    Murray, James
    Hubbard, Roderick E.
    Ohlson, Sten
    Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences. Nanyang Technol Univ, Sch Biol Sci, Singapore 637551, Singapore.
    Fragment Screening by Weak Affinity Chromatography: Comparison with Established Techniques for Screening against HSP902013In: Analytical Chemistry, ISSN 0003-2700, E-ISSN 1520-6882, Vol. 85, no 14, p. 6756-6766Article in journal (Refereed)
    Abstract [en]

    The increasing use of fragment-based lead discovery (FBLD) in industry as well as in academia creates a high demand for sensitive and reliable methods to detect the binding of fragments to act as starting points in drug discovery programs. Nuclear magnetic resonance (NMR), surface plasmon resonance (SPR), and X-ray crystallography are well-established methods for fragment finding, and thermal shift and fluorescence polarization (FP) assays are used to a lesser extent. Weak affinity chromatography (WAC) was recently introduced as a new technology for fragment screening. The study presented here compares screening of 111 fragments against the ATPase domain of HSP90 by all of these methods, with isothermal titration calorimetry (ITC) used to confirm the most potent hits. The study demonstrates that WAC is comparable to the established methods of ligand-based NMR and SPR as a hit-id method, with hit correlations of 88% and 83%, respectively. The stability of HSP90 WAC columns was also evaluated and found to give 90% reproducibility even after 207 days of storage. A good correlation was obtained between the various technologies, validating WAC as an effective technology for fragment screening.

  • 50. Mosbach, K
    et al.
    Glad, M
    Larsson, P O
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Affinity Precipitation (B) and High Performance Liquid Affinity Chromatography (C)1982Book (Other academic)
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