Independent education resourceInformation here does not replace care from a qualified health professional.
Peptide Therapy GuideClear peptide education

Educational guide

Odyssey Thera to Use GE Healthcare’s Imaging System

IN Cell Analyzer 6000 is expected to bolster use of high-content assays. Odyssey Thera has installed GE Healthcare’s IN Cell Analyzer 6000, a laser-based confocal imaging platform to advance its high-content assay capability. Odyssey Thera is leveraging system

Written by Peptide Therapy Guide Editorial Team
For education only

This guide cannot diagnose a condition or recommend a personal treatment plan. Discuss medical questions with a qualified professional.

IN Cell Analyzer 6000 is expected to bolster use of high-content assays.

Odyssey Thera has installed GE Healthcare’s IN Cell Analyzer 6000, a laser-based confocal imaging platform to advance its high-content assay capability. Odyssey Thera is leveraging systems biology to decipher biologically relevant pathways in human cells. The firm’s cell-based technologies include protein-fragment complementation assays (PCAs) that allow protein-protein complexes to be precisely imaged and localized within live cells.

Using PCA and other technologies, Odyssey says that it has created the largest high-content assay capability. Fully integrated hardware, software, and IT infrastructure enables very high throughput, creating a systems- and chemical-biology platform capable of capturing and analyzing hundreds of thousands of microscopic images per day, the company adds.

The IN Cell Analyzer 6000 employs a unique optical engine combined with a next-generation sCMOS detector to support high-throughput and high-resolution imaging of diverse biological events. In contrast to conventional fixed aperture confocal systems, the IN Cell Analyzer 6000 optical system features a fully adjustable variable aperture for increased flexibility.

“The IN Cell 6000 is designed for the most demanding high-content cellular applications including live-cell assays, 3-D imaging, co-localization studies, and imaging of assays with low signal,” remarks John K. Westwick, Ph.D., president and CEO of Odyssey Thera. “The choice of GE Healthcare’s IN Cell 6000 reflects Odyssey’s goal of maintaining our leadership position in highly contextual cellular analysis.”

Jane E. Lamerdin, Ph.D., executive director of R&D at Odyssey Thera, says, “The Odyssey team will use the IN Cell 6000 for multiple projects including advancement of partner drug discovery programs and collaborative work with the United States Environmental Protection Agency (EPA), in which methods are being developed to improve detection of environmental toxicants.”

Most recently, in March 2010, Lonza signed on to provide Odyssey’s PCA technology to researchers as part of its compound-profiling services. Additionally, Odyssey Thera granted Lonza an option to certain exclusive, global technology licenses. The companies have also initiated collaborative technology, product development, and marketing activities. In May 2009, Odyssey entered a collaboration to analyze Mitsubishi Tanabe Pharma’s preclinical drug candidates using its PCA technology.

Prior to 2008, Odyssey had inked partnerships with the likes of Abbott, Bristol-Myers Squibb, Merck & Co., Pfizer, and Roche. The company has reported most on progress made in the Pfizer collaboration. The latest update was that the firms had published a paper in PNAS describing a the use of Odyssey’s platform for optimizing Pfizer’s PAK inhibitor anticancer agent called PF-3758309.

Back in October 2009 Odyssey reported on the achievement of a milestone fee from Pfizer following Pfizer’s decision to progress drug candidates studied by Odyssey Thera as part of their multiyear alliance intiated in August 2006. Those milestones were reportedly the company’s fourth and fifth to be earned.

Connected reading

Helpful context for this guide

Source-derived material selected through this article’s indexed topics.

Related questions

01Undruggable or unscreenable?

Another obstacle to discovering new PPI inhibitors is the lack of libraries designed to hunt for them, points out Philippe Roche, PhD, senior scientist at the Integrative Structural and Chemical Biology team at the Cancer Research Center of Marseilles, France. “If you screen PPIs using libraries that were designed for kinases or GPCRs, that’s why you don’t get a lot of good results,” he says. To that end, his group began assembling a library focused on orthosteric inhibitors of PPIs. The result was 2P2Idb, a hand-curated, structural database cataloguing orthosteric inhibitors of PPIs for which the interface had been 3D characterized. From analyzing these known PPI inhibitors, and what structures they had in common, Roche and his colleagues developed a model to predict whether compounds would likely inhibit PPIs. Using this method, 2P2Idb creates an enriched screening library that dramatically increases the hit rate compared to standard libraries. Having proven their success with a small library of 1600 compounds, they are in the process of expanding the library to 10,000 compounds. Once that’s published, “the idea is to make this library available to labs around the world,” Roche says. “We will provide the library free of charge for people to be able to screen PPI targets.”

Source: www.genengnews.com ↗
02How stable is the antibody?

A crucial question often addressed during preclinical development focuses on the in vivo stability of therapeutic antibodies. Increasing the half-life of a therapeutic antibody has several benefits ranging from higher treatment efficacy to increased advantages for the patients who will have a fewer number of therapy sessions and a reduced cost. Given these compelling benefits, following the identification of therapeutic antibodies with the desired specificity, developers usually subject them to a refinement step to increase their stability. This process is often hindered by the lack of reliable experimental tools to predict the half-life of antibodies in patients. The major hurdle of using mouse models to predict antibody stability in the serum lies in the way immunoglobulin proteins are processed by the organism. In mammals, most proteins circulating in the serum undergo constant uptake by endothelial cells and are routed through the endosomes to the lysosomal compartment for degradation. In the endosomes, immunoglobulin G (IgG) proteins are recognized and bound by a transmembrane protein, called the neonatal Fc receptor (FcRn), which mediates their recycling to the plasma membrane and subsequent release back into the serum. As a result, the half-life of IgGs are significantly extended by this mechanism. Since most therapeutic antibodies belong to the IgG class, this recycling system is very relevant for their relative stability in the body. Remarkably, the relative affinity between IgGs and FcRn is extremely disparate between different species, with the mouse receptor showing a much higher affinity than its human counterpart.

Source: www.genengnews.com ↗
P

About the author

Peptide Therapy Guide Editorial Team

Editorial team for Peptide Therapy Guide.

View all articles →

Continue learning

Related guides