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  • 1.
    Bergström, Maria
    University of Kalmar, Department of Chemistry and Biomedical Sciences.
    Analytical affinity separations based on weak protein - carbohydrate interactions2006Doctoral thesis, monograph (Other academic)
  • 2.
    Bergström, Maria
    et al.
    Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences.
    Ganji, Suresh
    Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences.
    Naidu Veluru, Ramesh
    Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences.
    Unelius, C. Rikard
    Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences.
    N-Iodosuccinimide (NIS) in Direct Aromatic Iodination2017In: European Journal of Organic Chemistry, ISSN 1434-193X, E-ISSN 1099-0690, no 22, p. 3234-3239Article in journal (Refereed)
    Abstract [en]

    N-Iodosuccinimide (NIS) in pure trifluoroacetic acid (TFA) offers a time-efficient and general method for the iodination of a wide range of mono-and disubstituted benzenes at room temperature, as demonstrated in this paper. The starting materials were generally converted into mono-iodinated products in less than 16 hours at room temperature, without byproducts. A few deactivated substrates needed addition of sulfuric acid to increase the reaction rate. Another exception was methoxybenzenes that preferentially were iodinated by NIS in acetonitrile with only catalytic amounts of TFA.

  • 3.
    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.

  • 4.
    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)
  • 5.
    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)
  • 6.
    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)
  • 7.
    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.

  • 8.
    Boman, Sara
    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.
    Blücher, Anna
    Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences.
    Håkansson, Andreas
    Kristianstad university.
    Andersson, Håkan S.
    Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences.
    Dietary habits of Swedish university students in nutrition science between 2001 and 20162016In: Abstracts. The 11th NORDIC NUTRITION CONFERENCE NNC2016. “Bridging nutrition sciences for better health in the Nordic countries”, 2016, article id P470Conference paper (Other academic)
    Abstract [en]

    While the Swedish nutrition recommendations have been kept relatively constant in recent years, public attitudes to different diets have been swinging faster. The National food survey (Riksmaten), being performed in Sweden only once per decade, cannot identify any corresponding rapid changes in diets. Hence, our understanding of potential fluctuations is limited. During the last 15 years, nutrition students at the Linnaeus University (formerly University of Kalmar) have reported their food intake in the context of the course Diet, Nutrition and Health 7,5 hp. The result is an extensive data set comprising more than 1100 individuals and over 2500 days of food intake reports, and although not originally intended or designed as a study, it became apparent that these data could be of interest as an indicator for national dietary trends. Food intake was reported (by weighing or estimating the amounts) for two weekdays and one weekend day per student, along with age, length, sex and weight. Food intake was translated to nutrient intake using Dietist Net software (Kost & Näringsdata).  Admittedly, the data set has some validity problems: the students differ from the Riksmaten study groups in mean age and geographical distribution, and all data was collected during March-April. As students in a nutrition course, they can also be expected to be more interested and more knowledgeable in the nutrition subject than the average person. Nevertheless, the results clearly demonstrate a substantial change in nutrient intake from 2006 and onwards, where the energy from carbohydrates decreased from above 50% to below 40%, and where the energy intake from fat increased from about 25% to 36%. Further details, such as the effects on the intake of selected micronutrients, will be presented.

  • 9. Cheshev, Pavel
    et al.
    Morelli, Laura
    Marchesi, Marco
    Podlipnik, Crtomir
    Bergström, Maria
    Linnaeus University, Faculty of Science and Engineering, School of Natural Sciences.
    Bernardi, Anna
    Synthesis and affinity evaluation of a small library of bidentate cholera toxin ligands: towards nonhydrolyzable ganglioside mimics2010In: Chemistry - A European Journal, ISSN 0947-6539, E-ISSN 1521-3765, Vol. 16, no 6, p. 1951-1967Article in journal (Refereed)
    Abstract [en]

    A small library of nonhydrolyzable mimics of GM1 ganglioside, featuring galactose and sialic acid its pharmacophoric carbohydrate residues,, was synthesized and tested. All compounds were synthesized from readily available precursors using high-performance reactions, including click chemistry protocols, and avoiding O-glycosidic bonds. Sonic of the most active molecules also feature a point of further derivatization that can be used for conjugation will, polyvalent aglycons. Their affinity towards cholera toxin was assessed by weak affinity chromatography, which allowed a systematic evaluation and selection of the best candidates. Affinity could be enhanced up to one or two orders of magnitude over the affinity of the individual pharmacophoric sugar residues.

  • 10.
    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.

  • 11.
    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.

  • 12.
    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.

  • 13.
    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.

  • 14.
    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.

  • 15.
    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.

  • 16.
    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.

  • 17. 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)
  • 18.
    Nilsson, Mikael
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Harang, V
    Bergström, Maria
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Ohlson, Sten
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Isaksson, Roland
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Johansson, G
    Determination of Protein-Ligand Affinity Constants from Direct Migration Time in Capillary Electrophoresis2004In: Electrophoresis, Vol. 25, p. 1829-1836Article in journal (Refereed)
  • 19.
    Ohlson, Sten
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Bergström, Maria
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Leickt, Lisa
    Zopf, David
    Weak affinity chromatography of small saccharides with immobilised wheat germ agglutinin and its application to monitoring of carbohydrate transferase activity1998In: Bioseparation, Vol. 7, p. 101-106Article in journal (Refereed)
  • 20.
    Ohlson, Sten
    et al.
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Bergström, Maria
    University of Kalmar, School of Pure and Applied Natural Sciences.
    Påhlsson, Peter
    Lundblad, Arne
    Use of monoclonal antibodies for weak affinity chromatography1997In: Journal of Chromatography A, Vol. 758, p. 199-208Article in journal (Refereed)
  • 21.
    Ohlson, Sten
    et al.
    Linnaeus University, Faculty of Science and Engineering, School of Natural Sciences.
    Duong-Thi, Minh-Dao
    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
    Hansson, Lennart
    Pedersen, Lennart
    Guazotti, Sergio
    Isaksson, Roland
    Linnaeus University, Faculty of Science and Engineering, School of Natural Sciences.
    Toward high-throughput drug screening on a chip-based parallell affinity separation platform2010In: Journal of Separation Science, ISSN 1615-9306, E-ISSN 1615-9314, Vol. 33, no 17-18, p. 2575-2581Article in journal (Refereed)
    Abstract [en]

    High-throughput screening of compound libraries, including the study of fragments, has become one of the cornerstones in modern drug discovery research. During this process hits are defined that may be developed into valuable leads and eventually into possible drug candidates. In this paper, we have demonstrated that parallel zonal weak affinity chromatography in microcolumns on a chip offers a possible screening format for weakly binding ligands toward a protein target. We used albumin as a model system because this transport protein is well established as a binder (both weak and strong) for drug substances. Bovine serum albumin was immobilized on microparticulate diolsilica particles and then packed into a 24-channel cartridge, which served as the separation platform. Analysis of the obtained chromatograms yielded information about affinity even in the millimolar range. Employing this approach, thousands of substances can be screened in just a day. We feel confident that zonal affinity chromatography will provide a useful technology in the future for performing high-throughput screening.

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