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  • 1.
    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.

  • 2.
    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.

  • 3.
    Ohlson, Sten
    et al.
    Perstorp Biolytica AB, S-223 70, Lund, Sweden.
    Lundblad, Arne
    Zopf, David
    Novel Approach to Affinity Chromatography Using "Weak" Monoclonal Antibodies1988In: Analytical Biochemistry, ISSN 0003-2697, E-ISSN 1096-0309, Vol. 169, no 1, p. 204-208Article in journal (Refereed)
    Abstract [en]

    Affinity purification generally relies on specific high-affinity recognition between two species of biological molecules: one molecular species (the ligate) dissolved in a mobile phase is selectively adsorbed to the other species (the ligand) coupled to a solid support. Desorption of the ligate often requires harsh conditions that degrade biological activity of the purified product. As an alternative to this general procedure, we have studied affinity chromatography in a weak affinity mode, where ligand-ligate interactions are in dynamic equilibrium. Ligates recognized with low affinities (dissociation constant > 104 ) elute from affinity columns under mild, isocratic conditions as retarded peaks, separated from noninteracting solutes that elute in the void volume. To illustrate the procedure, we report chromatography of an oligosaccharide on a 2-ml column containing 86 mg of a monoclonal antibody coupled to 10-μm microparticulate silica particles. Using a temperature-sensitive antibody, we observed that when the ligand-ligate dissociation constant is > 10−3 , performance of the system exceeds 300 theoretical plates/10 cm column length and approaches the efficiencies generally associated with high-performance liquid chromatography. 

  • 4.
    Ušaj, Marko
    et al.
    Technion - Israel Institute of Technology, Israel.
    Zattelman, Lilach
    Technion - Israel Institute of Technology, Israel.
    Regev, Ronit
    Technion - Israel Institute of Technology, Israel.
    Shneyer, Boris I.
    Technion - Israel Institute of Technology, Israel.
    Wiesel-Motiuk, Naama
    Technion - Israel Institute of Technology, Israel.
    Henn, Arnon
    Technion - Israel Institute of Technology, Israel.
    Overexpression and purification of human myosins from transiently and stably transfected suspension adapted HEK293SF-3F6 cells2018In: Analytical Biochemistry, ISSN 0003-2697, E-ISSN 1096-0309, Vol. 558, no 1, p. 19-27Article in journal (Refereed)
    Abstract [en]

    The myosin family of motor proteins is an attractive target of therapeutic small-molecule protein inhibitors and modulators. Milligrams of protein quantities are required to conduct proper biophysical and biochemical studies to understand myosin functions. Myosin protein expression and purification represent a critical starting point towards this goal. Established utilization of Dictyostelium discoideum, Drosophila melanogaster, insect and mouse cells for myosin expression and purification is limited, cost, labor and time inefficient particularly for (full-length) human myosins. Here we are presenting detailed protocols for production of several difficult-to-purify recombinant human myosins in efficient quantities up to 1 mg of protein per liter of cell culture. This is the first time that myosins have been purified in large scales from suspension adapted transiently and stably expressing human cells. The method is also useful for expressing other human proteins in quantities sufficient to perform extensive biochemical and biophysical characterization.

  • 5. Wang, W T
    et al.
    Kumlien, J
    Ohlson, Sten
    Perstorp Biolytica AB, Lund.
    Lundblad, Arne
    Zopf, David
    Analysis of a Glucose-Containing Tetrasaccharide by High-Performance Liquid Affinity Chromatography1989In: Analytical Biochemistry, ISSN 0003-2697, E-ISSN 1096-0309, Vol. 182, no 1, p. 48-53Article in journal (Refereed)
    Abstract [en]

    In the present work we have explored conditions for using a pulsed amperometric detector for on-line analysis of oligosaccharides eluted from a high-performance liquid affinity chromatography column. A monoclonal antibody that specifically binds a glucose-containing oligosaccharide is coupled to a SelectiSphere-10-activated tresyl column. The system is eluted isocratically and easily detects 10 ng of the oligosaccharide with a linear response up to 250 ng. Analysis of both serum and urine samples from normal individuals and patients with acute pancreatitis gives a single retarded peak with a retention time identical to that of authentic (Glc)4. Retarded material pooled from several analyses of urine was positively identified as (Glc)4 by GC-MS analysis. As this method requires little cleanup and no chemical derivitization of the sample and is performed rapidly (less than 20 min) at sensitivities of at least 10μg/liter in biological fluids, it represents a substantial improvement over previous GC-MS, radioimmunoassay, and enzyme-linked immunoadsorbent assay methods used to determine (Glc)4. 

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