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The Latest in Biopharm Discovery, Development, and Bioprocessing

ForteBio systems have become indispensable tools at biopharmaceutical companies worldwide, resulting in a steady stream of scientific publications and presentations. This online resource will help you stay current on the latest studies featuring data from the Octet® and BLItz® systems. Fresh publications and presentations are captured as they become available, and can be browsed by application area or pinpointed by keyword search.

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  • Exploiting a Water Network to Achieve Enthalpy-driven, Bromodomain-selective BET Inhibitors
    Shadrick WR, et al., Bioorg Med Chem, 26(1):25-36, 2018
    The Bromodomain and Extra-Terminal domain family (BET) of proteins are potential therapeutic targets in a wide range of diseases including oncology, auto-immune disease, heart failure, and male contraception. The BET family of proteins comprises of BRD2, BRD3, BRD4, and BRDT, which are distinguished by the presence of two tandem bromodomains (BD1 and BD2). All BRDs have four alpha-helices that are tethered together by two loop regions (ZA and BC) of variable length and sequence. Described herein is the design and synthesis of a congeneric series 2- and 3-heteroaryl substituted tetrahydroquinolines (THQs) in order to exploit various water networks in the ZA channel of bromodomains to achieve enthalpy-driven, bromodomain-selective BET inhibitors. Binding affinity of each compound to both BRD2 bromodomains (BRD2-BD1 and BRD2-BD2) was investigated by Surface Plasmon Resonance (SPR) using a Pall ForteBio Pioneer instrument equipped with a HisCap sensor chip. The HisCap sensor surface was activated with nickel ions. Poly-His tagged BRD2 constructs were immobilized onto sensor chip surface by capture-coupling, a hybrid method of capture and amine coupling chemistry. Each compound was prepared in running buffer as a 3-fold dilution series and were injected in duplicate at each concentration. The SPR data obtained were processed and globally fitted to a 1:1 binding model. The kinetic rate constants (ka and kd) and the equilibrium dissociation constants (KD) were determined for all binding interactions. Overall results of this investigation suggest that the optimization of BD2-selective compounds has great implications for the development of promising clinical candidates.


  • N6L Pseudopeptide Interferes with Nucleophosmin Protein-protein Interactions and Sensitizes Leukemic Cells to Chemotherapy
    De Cola A, et al., Cancer Letters, 412:272-282, 2018
    Nucleophosmin (NPM1) is a nucleolar phosphoprotein, which plays key structural and functional roles including centrosome duplication, rRNA biogenesis and maturation, DNA damage response and chaperone activity. In one third of acute myeloid leukemia (AML) patients, NPM1 is aberrantly localized in the cytoplasm. It is believed that this "wrong" cytoplasmic localization of NPM1 obstruct the tumor suppressive mechanisms. The anticancer molecule NucAnt 6L (N6L) is a synthetic pseudopeptide which has been shown to interact with NPM1. Investigated herein are the interaction of N6L with NPM1 and the antitumor effect of N6L on AML cell lines. The binding interaction between N6L and NPM1 was studied by using Surface Plasmon Resonance (SPR). A Pall ForteBio Pioneer instrument equipped with a Streptavidin-coated BioCap sensor chip was used to perform all SPR experiments. Biotinylated N6L was immobilized onto sensor chip surface. Both human full length NPM1 and its isolated N-terminal domain were injected in increasing concentrations. SPR data obtained were globally fitted using two-site and three-site binding models. Equilibrium dissociation constants (KD) were determined for all binding interactions between N6L and NPM1 constructs. Overall results of this study demonstrate that N6L interferes with NPM1 protein-protein interactions and sensitizes AML cells to chemotherapy, suggesting that N6L may have important implications for the development of AML therapies.


  • Galectin-13, a Different Prototype Galectin, does not Bind β-galacto-sides and Forms Dimers via Intermolecular Disulfide Bridges Between Cys-136 and Cys-138
    Su J, et al., Sci Rep., 8(1):980, 2018
    Galectin-13 (Gal-13) is a prototype galectin. It is predominantly expressed in the placenta and plays a key role in pregnancy. Reported herein are the crystal structure of Gal-13 and the discovery of its structure-function relationships using biochemical and cellular studies. Bio-Layer Interferometry (BLI) was used to assess binding affinities of Gal-13 and Gal-3 towards polysaccharides, including ginseng pectin RG-I-4 (a type of rhamnogalacturonan I pectin). A Pall ForteBio Octet RED96 system equipped with Ni-NTA (NTA) Biosensor probes was used to perform all BLI experiments. His-tagged Gal-3/His-tagged Gal-13 was immobilized onto NTA sensor tips. Loaded sensor tips were then dipped in wells containing different concentrations of polysaccharide samples. Data were fitted using 1:1 binding model. Equilibrium dissociation constants (KD) were determined. Overall results of this investigation suggest that galectin-13 is a new type of prototype galectin with unique properties.


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