Bruker Announces Release of Breakthrough CaptiveSpray(TM) Nano/Capillary Electrospray Ion Source for Proteomics at ASMS 2011

At ASMS 2011, Bruker is introducing the breakthrough, proprietary CaptiveSpray electrospray ion source for nano-HPLC applications in proteomics. Using CaptiveSpray technology in many cases increases bottom-up protein identifications significantly, and CaptiveSpray is presently the best available technology for robust, reproducible protein ID or quantitative proteomics applications, with excellent, stable sensitivity over long time periods.
Unlike a traditional pulled nanospray tip, the Etch-Taper™ technology employed by CaptiveSpray ensures that the internal diameter of the spray tip remains constant, thereby reducing tip clogging, and providing excellent spray stability over the entire LC gradient and robust operation for long time periods, even with heavy proteomics samples loads. A key proprietary feature of the CaptiveSpray is its novel gas-flow focusing technology for dramatic sensitivity gains compared to normal electrospray. The CaptiveSpray source delivers nanospray sensitivity without the need for complex and time consuming spray tip adjustments, while its innovative plug-and-play design fits all current Bruker LC-MS instruments, including the latest maXis UHR-Qq-TOF systems, solariX FTMS systems and amaZon ETD ion trap mass spectrometers. 
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Natural Language Processing to Play Major Role in Bringing Watson into Clinics

Under the terms of a recently inked agreement between IBM And Nuance, Watson's deep question answering, natural language processing, and machine learning capabilities will be linked with Nuance's speech recognition and Clinical Language Understanding, CLU, solutions to help physicians more accurately diagnose and treat their patients (BI02/11/2011).

In the months leading up to the first offerings from the collaboration, researchers at IBM and Nuance will work with collaborators at Columbia University and the University of Maryland, to figure out how Watson can best help in the clinical setting as well as to incorporate some healthcare-specific adaptations to the system, Jennifer Chu-Carroll, a member of the Watson Research Team, told BioInform.

"For the most part, the natural language analytics, the machine learning and the whole architecture are domain independent so we expect to be able plug these into the medical domain," she said. However, "there [will] be some ... research and development that is specific to the medical domain that we are going to have to bring in."

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Research scientists develop powerful new methodology for stabilizing proteins

A team of scientists at The Scripps Research Institute has discovered a new way to stabilize proteins - the workhorse biological macromolecules found in all organisms. Proteins serve as the functional basis of many types of biologic drugs used to treat everything from arthritis, anemia, and diabetes to cancer.

As described in the February 4, 2011 edition of the journal Science, when the team attached a specific oligomeric array of sugars called a "glycan" to proteins having a defined structure, the proteins were up to 200 times more stable in the test tube. In the body, this stability may translate into longer half-lives for therapies, possibly lowering the overall cost of treatment for certain protein-based drugs and requiring patients to have fewer injections during a course of treatment.

The work may have major implications for the drug industry because there are a large number of protein-based drugs on the market, more in clinical trials, and many more under development worldwide. Nearly all of these protein-based drugs have glycans attached to them and are therefore called "glycoproteins". Glycoprotein-based drugs can be quite expensive to produce and usually need to be administered intravenously.

One of the challenges in producing these drugs has been increasing their stability, which generally extends their half-life in the bloodstream - issues that the new discovery appears to address directly.

"We've now provided engineering guidelines for glycoprotein stability," said Scripps Research Professor Jeffery W. Kelly, who is chair of the Department of Molecular and Experimental Medicine, Lita Annenberg Hazen Professor of Chemistry, and member of The Skaggs Institute for Chemical Biology at Scripps Research. Kelly led the study with Scripps Research Associate Professor Evan Powers and Staff Scientist Sarah R. Hanson, in collaboration with Research Associates Elizabeth K. Culyba, Joshua Price, and colleagues.

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University Uses Thermo Fisher Scientific ICP-MS for Reliable and Efficient Sulfur Detection in Proteins

"Thermo Fisher Scientific Inc. announced that the University of Oviedo’s analytical spectrometry research group has implemented the Thermo Scientific XSERIES 2 ICP-MS to perform reliable and interference-free sulfur detection in proteins.

The analytical spectrometry research group at the University of Oviedo in Asturias, Spain aims to solve the analytical challenges encountered by science and technology. Within this framework, a small sub-group has been established focusing on the development of inductively coupled plasma-mass spectrometry (ICP-MS) based analytical methods for the quantification of biopolymers such as DNA and proteins. One of the principal issues faced by the group is the interference from gas-based polyatomics such as oxygen in the determination of sulfur when using a low resolution instrument. To eliminate these problems, the group selected the Thermo Scientific XSERIES 2 ICP-MS with collision/reaction cell technology (CRC).

Quantitative protein analysis is currently one of the most demanding applications in analytical chemistry. Mass spectrometric techniques such as electrospray ionization-mass spectrometry (ESI-MS) and matrix assisted laser desorption ionization-mass spectrometry (MALDI-MS) have traditionally played a key role in protein analysis. However, the potential of ICP-MS has recently been recognized for the determination of proteins. Although ICP-MS detection does not provide any structural information, its outstanding capability to quantify most of the elements proves valuable for accurate protein quantification. Keeping pace with the latest technological developments, the University of Oviedo’s research group has coupled the XSERIES 2 ICP-MS with a reversed-phase capillary liquid chromatography (μLC) system to facilitate precise determination of sulfur isotopes in standard proteins.

Dr. Jörg Bettmer of the University of Oviedo’s analytical spectrometry research group comments, “The Thermo Scientific XSERIES 2 ICP-MS was chosen because no other quadrupole-based system matches its capabilities in terms of accuracy, reliability and overall efficiency. The implementation of the instrument has allowed us to achieve reliable, interference-free detection of sulfur isotopes. It has enabled us to determine sulfur-containing standard proteins in an accurate and efficient manner that had not been previously possible.”

The XSERIES 2 offers outstanding productivity in a quadrupole ICP-MS for both routine and high-performance analytical applications. By using the system, laboratories can achieve their analytical objectives faster, with greater confidence and less hands-on time from the operator. The innovative ion lens design of the instrument enables simple field upgrade to collision cell technology (CCT) performance without affecting the normal (non-CCT mode) sensitivity or background. The cell is also compatible with a range of reactive gases, such as pure oxygen for interference suppression in challenging matrices."

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Clinical proteomics for liver disease: a promising approach for discovery of novel biomarkers

Hepatocellular carcinoma (HCC) is the fifth most common cancer and advanced hepatic fibrosis is a major risk factor for HCC. Hepatic fibrosis including liver cirrhosis and HCC are mainly induced by persistent hepatitis B or C virus infection, with approximately 500 million people infected with hepatitis B or C virus worldwide. Furthermore, the number of patients with non-alcoholic fatty liver disease (NAFLD) has recently increased and NAFLD can progress to cirrhosis and HCC. These chronic liver diseases are major causes of morbidity and mortality, and the identification of non-invasive biomarkers is important for early diagnosis. Recent advancements in quantitative and large-scale proteomic methods could be used to optimize the clinical application of biomarkers. Early diagnosis of HCC and assessment of the stage of hepatic fibrosis or NAFLD can also contribute to more effective therapeutic interventions and an improve prognosis. Furthermore, advancements of proteomic techniques contribute not only to the discovery of clinically useful biomarkers, but also in clarifying the molecular mechanisms of disease pathogenesis by using body fluids, such as serum, and tissue samples and cultured cells. In this review, we report recent advances in quantitative proteomics and several findings focused on liver diseases, including HCC, NAFLD, hepatic fibrosis and hepatitis B or C virus infections.

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