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The Latest in Biopharm Discovery, Development, and Bioprocessing

Pall 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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  • Inhibition of Pax2 Transcription Activation with a Small Molecule that Targets the DNA Binding Domain
    Grimley E, et al., ACS Chem Biol, 12(3):724-734, 2017
    The Pax gene family represents crucial embryonic developmental control genes that encode DNA binding transcription factors. In vertebrates, Pax2 plays a key role in the development of the kidney and the reproductive systems. Authors hypothesize that Pax2 could be an excellent target in the development of therapeutics for renal diseases. Described herein is the use of a homology model of the Pax2 paired domain and a structure based virtual screening to identify small molecules that can inhibit Pax2 transcription activation by targeting the Pax2 DNA binding domain. The EG1 was identified as a compound that can effectively block Pax2 activity and the DNA binding. Binding affinity and kinetics of EG1 interacting with the Pax2 paired domain were studied using Bio-Layer Interferometry (BLI) with a Pall ForteBio Octet RED system. Biotinylated Pax2 protein was immobilized on to Streptavidin Biosensor probes. Subsequently, sensor tips were incubated in various concentrations of EGI. The binding buffer contained PBS with 0.1% DMSO. kon, koff, and KD values were determined by global fitting of the binding curves. A steady-state analysis of the binding curves (Req. vs. Concentration) provided an affinity constant consistent with that obtained from on- and off-rates. Overall results of this study suggest that the targeting of tissue-specific developmental control genes has a significant potential to minimize off-target activity and to be more effective in treatments.

    PubMed

  • Vesicular Stomatitis Virus N Protein-specific Single-domain Antibody Fragments Inhibit Replication
    Hanke L, et al., EMBO Rep, 18(6):1027-1037, 2017
    Vesicular stomatitis virus (VSV) single-stranded RNA genome is tightly encapsidated by nucleoprotein N to form a nucleocapsid (N-RNA). N-RNA serves as the template for RNA synthesis. In the absence of nucleoprotein N, full-length RNAs will not be produced and therefore nucleoprotein N is considered as a target of intervention of the virus life cycle. Described herein is the use of cytosolically expressed variable region of the heavy chain of camelid heavy-chain-only antibodies (VHHs) to target the viral nucleoprotein N. Four of the VHHs identified are specific for VSV. Affinity and kinetic parameters were determined by using Bio-Layer Interferometry (BLI). A Pall ForteBio Octet RED96 instrument equipped with Streptavidin Biosensor probes was used to perform all BLI experiments. Biosensor tips were loaded with biotinylated WT and escape mutant versions of N-RNA variants. Association and dissociation of VHHs were studied over a series of concentrations. Experimental data obtained were fitted using the 2:1 heterogeneous ligand binding global fit model. kon, koff, and KD values were determined. The binding sites on nucleoprotein N for some of the identified VHHs were characterized and the information was used to present a molecular explanation for the inhibitory effects of the N-specific VHHs. Overall, these findings reveal new features on the N protein surface that may have the potential to be used as an antiviral intervention options.

    PubMed

  • Tumor-secreted Anterior Gradient-2 Binds to VEGF and FGF2 and Enhances Their Activities by Promoting Their Homodimerization
    Guo H, et al., Oncogene, doi: 10.1038/onc.2017.132, 2017
    Human anterior gradient-2 (AGR2) is a protein that overexpresses in human adenocarcinomas. The exact function of secreted AGR2, including its mechanism of action is not well understood. Reported herein is the mechanism for the tumor-promoting function of extracellular AGR2. Furthermore, authors demonstrate that extracellular AGR2 directly binds to vascular endothelial growth factor (VEGF) and fibroblast growth factor 2 (FGF2) and amplify their activities. Binding affinity of AGR2 to various growth factors were studied by using the Bio-Layer Interferometry (BLI). A Pall ForteBio Octet RED96 instrument equipped with Ni-NTA biosensors was used to perform all BLI experiments. Biosensor tips were immobilized with His-AGR2. Subsequently, the AGR2-loaded biosensor tips were dipped in solutions of VEGF121, VEGF165, VEGF189, FGF2, EGF, IGF-1 and TGFβ1, respectively. KD values were determined for all the binding interactions. Collectively, findings of this investigation suggest that the secreted AGR2 is a promising antitumor target, which affects the function of extracellular signaling networks.

    PubMed

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