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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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  • Discovery and Characterization of Highly Potent and Selective Allosteric USP7 Inhibitors
    Gavory G, et al., Nat Chem Biol, 14(2):118-125, 2018
    Ubiquitin-specific protease 7 (USP7) is involved in multiple oncogenic pathways. Reported herein is the discovery and detailed characterization of highly potent and selective small molecule inhibitors of USP7. Authors demonstrate that the lead compounds identified in this study inhibit USP7 in a noncovalent and reversible manner. Furthermore, the first reports of high-resolution X-ray crystal structures of USP7 in complex with small-molecule inhibitors were also revealed. Small molecule inhibitors binding to USP7 were studied by Surface Plasmon Resonance (SPR) technology using a Pall ForteBio Pioneer system. The USP7 catalytic domain (residues 207-560) was expressed in E. coli cells. The purified proteins were immobilized onto the surface of the COOH5 sensor chip by using standard amine coupling chemistry. Subsequently, small molecule samples were diluted in running buffer and injected. SPR data obtained were analyzed using Qdat data analysis software. KD values were determined. Taken together, the results of this study demonstrate amenability and druggability of USP7 inhibitors and hence provides important insights for future target validation studies.


  • Interplay Between CedA, rpoB and Double Stranded DNA: A Step Towards Understanding CedA Mediated Cell Division in E. coli
    Sharma P, Tomar AK, and Kundu B, Int J Biol Macromol., 107(Pt B):2026-2033, 2018
    In DnaAcos mutant E. coli cells, cell division is inhibited due to excessive initiation of chromosomal replication. Previous studies suggest, Cell division activator (CedA), a double stranded-DNA binding protein, acts as a regulatory protein in DnaAcos mutants to begin cell division and regular colony formation. CedA is known to interact with various subunits of RNA polymerase complex, including rpoB. Reported herein are the mechanistic aspects of interactions between CedA, rpoB, and double stranded DNA (ds-DNA) by using a combination of biophysical and insilico experiments. The kinetics of the binding interaction of ds-DNA with CedA, rpoB, and CedA-rpoB complex was studied using Bio-Layer Interferometry (BLI). A Pall ForteBio Octet RED96 system equipped with Streptavidin (SA) Biosensor probes was used to perform all BLI assays. Biotinylated-DNA was immobilized on SA sensor tips. Association and dissociation kinetics of CedA, rpoB, and CedA-rpoB complex were studied. The binding data were globally fitted using 2:1 binding model. Kinetic parameters (kon and koff) and the KD values were determined for all binding interactions. Overall results of this study suggest that chromosome over-replication in E. coli signals CedA to recruit rpoB to specific DNA site(s), thereby initiating cell division.


  • The Use of a GroEL-BLI Biosensor to Rapidly Assess Preaggregate Populations for Antibody Solutions Exhibiting Different Stability Profiles
    Pace SE, et al., J Pharm Sci., 107(2):559-570, 2018
    Environmental stresses such as temperature, agitation, and light can cause protein-based drugs to aggregate to varying extents, thereby altering efficacy and safety. Described herein is the utility and pharmaceutical applicability of a previously reported chaperone GroEL-Bio Layer Interferometry (GroEL-BLI) based method to detect the formation of transiently formed, preaggregate species in therapeutic monoclonal antibody (mAb) samples. Four different therapeutic mAb candidates (2 IgG1 molecules, 1 IgG4 molecule, and 1 bispecific mAb) exposed to different environmental stresses were evaluated using an automated GroEL-BLI system. A Pall ForteBio Octet RED96 platform equipped with Streptavidin (SA) Biosensor probes was used to perform GroEL-BLI biosensor assays. Biotinylated GroEL was immobilized onto SA sensor tips. GroEL-SA biosensor tips were treated with BSA to minimize nonspecific binding of mAb to any unoccupied SA biosensor surfaces. Subsequently, the association and dissociation kinetics of antibodies (stressed or unstressed) were analyzed by dipping the GroEL loaded biosensor tips in various concentrations of antibody samples. Binding amplitudes (nm) at the association phase of each of the mAb samples were compared. ATP in an osmolyte mixture of urea and glycerol was used to remove bound antibody from GroEL. Overall results of this study suggest that this automated GroEL-BLI method can be used to rapidly identify preaggregate species in antibody solutions that exhibit different stability profiles.


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