Friday, July 8, 2011

Change in the Oxea management team

The global chemical company Oxea announces changes in leadership: For personal and family reasons, Neil Robertson, member of the management team of the Oxea Group and Managing Director of Oxea GmbH with responsibility for Finance, Accounting and IT, will retire at the end of 2011. This intention had already been communicated by the company last autumn.


To ensure a smooth transition, his successor Bernhard Spetsmann joined Oxea in October 2010 as a new member of the management team of the Oxea Group and as Managing Director of Oxea GmbH. Initially Spetsmann was responsible for Mergers & Acquisitions and strategic projects and has assumed increasing responsibility in the areas of Finance, Accounting and IT. He will assume complete responsibility for these areas from July 1, 2011.


As planned, Robertson will stay with Oxea until the end of the year. During this time his focus will be on strategic projects.


Before joining Oxea, Spetsmann was most recently CFO of Autobahn Tank & Rast GmbH. Prior to that he held several senior management positions at Schmalbach-Lubeca AG. Among others Spetsmann was CFO of the White Cap Division for Europe and Asia, and Head of Mergers & Acquisitions.


 

Chemist solves riddle of killer diseases

Anthrax, septicemia and meningitis are some of the planet's most deadly infections. In part because doctors lack basic insights to prevent and cure diseases caused by so called Gram-positive bacteria. Now, a chemist from the University of Copenhagen has revealed the mechanism behind these deadly infections.


By creating a synthetic version of a Gram-positive bacterial endotoxin, Danish synthetic chemist Christian Marcus Pedersen has made a contribution that'll compel immune biologists to revise their textbooks. More importantly, he has paved the first steps of the way towards new and effective types of antibiotics.


Chemist in international collaboration with biologists and physicians


The research results were attained in collaboration with Prof. Richard R. Schmidt of the University of Konstanz and biologists at the Leibniz-Zentrum für Medizin und Biowissenschaften in Borstel, Germany. Ulrich Zähringer, leader of the Center in Borstel, is thrilled with Pedersen's achievement.


"No one knew what substance Gram-positive bacteria released to make us sick. But because Pedersen can supply us with substances that are entirely pure, and have a known structure and composition, we are able to get a more precise answer as to why we show symptoms when these bacteria enter our body," explains Professor Zähringer.


Synthesis succeeds where biologists gave up


Lipoteichoic acid, is a substance created and present in the cell wall of Gram positive bacteria. It appears to be the culprit of stimulating immune response symptoms such as fever, inflammation and organ failure. Indeed, when exploring illness, it is critical to investigate the substances that bind themselves to healthy human cells and thus, the cell wall becomes an important place to look. But if the substance breaks down as soon as it comes under the microscope, the chances of studying its binding abilities are not very great. Therefore, it was a major breakthrough when Pedersen was able to fabricate the molecule from scratch.


"Biologists have been trying to isolate this poison from living organisms for years. But the substance has a number of active groups. That is to say, the spiked parts of the molecule which enable the entire molecule to bind to cells. This makes it extremely difficult to purify. And dirty molecules are not conducive to viable research. Therefore, it's a great advantage to fabricate the substance synthetically, because we can "build" a molecule in which everything is included... Or where we ourselves decide which part of the structure to leave out," says Christian Marcus Pedersen.


Tiresome task but outstanding results


Lipoteichoic acid consists of 335 atoms combined in tangle, the complexity of which has made it difficult to collect. To create pure and intact molecules, Pedersen needed to complete 88 so-called synthesis steps. That is to say that 88 distinct "recipes", all of which needed to function, were required in order to reach the final result. These synthetic biomolecules are a fantastic tool for biologists in the investigation of Gram-positive bacteria's attack mechanisms.


"When it comes to these bacteria, there is still no one who knows precisely what on the bacteria activates the immune system. But we can build the precise parts of the structure that we want to. And biologists can examine how what we have built reacts with the immune system," says Pedersen.


Provided by University of Copenhagen

2010 much better year for container glass production

06-30-2011: Production data 2010 published from the European Container Glass Federation (FEVE)  show a general recovery from the drop of the previous year. In 2010, the European industry produced 20.7 million tonnes of glass compared to 20.1 million tonnes in 2009 marking an increase of 3.5%.

The biggest increase in production was recorded in Turkey (27%) and United Kingdom (9.5%). In Italy (5.2%), Poland (5.7%) the increase was more important than in Portugal (1.9%), Spain (2.7%) and North & Central countries (1.7%). In Germany the situation was stable (0.2%) as well as in France where a slight decrease was recorded (-0.1%).

“The industry was able to react firmly to the impact of the previous year’s financial crisis – says FEVE President Niall Wall – and to maintain its place as a key player in the packaging market notwithstanding the harsh competition. This is important if we are to offer consumers choice because glass is their preferred packaging thanks to its environmental, health and taste preservation qualities.  For some natural and healthy products like milk, yoghurts, baby food or mineral waters, consumer demand for glass packaging is not being met because of the lack of choice on supermarket shelves”.

The industry continues to make efforts to improve the efficiency of manufacturing process, to reduce environmental impacts and to reduce costs to ensure that brands are provided with a premium packaging solution at competitive prices when compared to other materials.

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Iowa State hybrid lab combines technologies to make biorenewable fuels and products

Laura Jarboe pointed to a collection of test tubes in her Iowa State University laboratory.


Some of the tubes looked like they were holding very weak coffee. That meant microorganisms – in this case, Shewanella bacteria – were growing and biochemically converting sugars into hydrocarbons, said Jarboe, an Iowa State assistant professor of chemical and biological engineering.


Some of the sugars in those test tubes were produced by the fast pyrolysis of biomass. That's a thermochemical process that quickly heats biomass (such as corn stalks and leaves) in the absence of oxygen to produce a liquid product known as bio-oil and a solid product called biochar. The bio-oil can be used to manufacture fuels and chemicals; the biochar can be used to enrich soil and remove greenhouse gases from the atmosphere.


Iowa State's Hybrid Processing Laboratory on the first floor of the new, state-built Biorenewables Research Laboratory is all about encouraging that unique mix of biochemical and thermochemical technologies. The goal is for biologists and engineers to use the lab's incubators, reactors, gas chromatography instruments and anaerobic chambers to find new and better ways to produce biorenewable fuels and chemicals.


"Biological processes occur well below the boiling point of water, while thermal processes are usually performed hundreds of degrees higher, which makes it hard to imagine how these processes can be combined," said Robert C. Brown, an Anson Marston Distinguished Professor in Engineering, the Gary and Donna Hoover Chair in Mechanical Engineering, and the Iowa Farm Bureau Director of Iowa State's Bioeconomy Institute.


"In fact, these differences in operating regimes represent one of the major advantages of hybrid processing," Brown said. "High temperatures readily break down biomass to substrates that can be fermented to desirable products."


Jarboe's research is one example. She's trying to develop bacteria that can grow and thrive in the chemicals and compounds that make up bio-oil. That way, they can ferment the sugars from bio-oil with greater efficiency and produce more biorenewable fuels or chemicals.


Another example of mixing the biochemical with the thermochemical is the work of Zhiyou Wen, an associate professor of food science and human nutrition, and Yanwen Shen, a doctoral student in his research group.


They're working to break down a bottleneck in the fermentation of synthesis gas – a mixture of carbon monoxide and hydrogen that's produced by the partial combustion of biomass in a gasifier. The fermentation process slows when researchers dissolve the gas into a liquid that can be used by to produce biofuels. They're looking for bioreactor technologies that boost the mass transfer of the synthesis gas without adding energy costs.


A third example is the work of DongWon Choi, a former doctoral student and post-doctoral research associate at Iowa State who's now an assistant professor of biological and environmental sciences at Texas A&M University Commerce. He continues to collaborate in the hybrid lab by working with microalgae that convert carbon dioxide into oil that can be used to produce biofuels.


That oil is currently harvested with solvents or mechanical presses. Both processes produce a lot of waste and the resulting waste management problems. Choi is using pyrolysis technology to heat the algae and convert it into jet and diesel fuels without the waste.


And the researchers say the hybrid lab's mix of people, technologies, equipment and ideas is beginning to show results.


"The hybrid lab provides enormous opportunities for performing biological-based processes for producing biofuel from thermochemically treated biomass," Wen said.


Yes, said Jarboe, "I think it is working well. This is a long process, but we're writing research proposals and papers. Everybody loves the idea of this hybrid approach. It has such a promising future; the challenge is in the collaboration."


The hybrid lab is starting to make the collaboration easier, though.


Brown said he's noticed the students who work in the hybrid lab seem to be comfortable crossing thermochemical and biochemical lines: "Just like children from different cultures often learn to communicate with one another more quickly than do their parents, graduate students seem to pick up cross disciplinary culture and language faster than their faculty advisers."


Provided by Iowa State University (news : web)

Click chemistry creates new 'stealth' DNA links

Scientists at the University of Southampton have pioneered a chemical method of linking DNA strands that is tolerated by living organisms.


The researchers have developed an artificial DNA "stealth" linkage using click chemistry, a highly-efficient chemical reaction, to join together DNA strands without disrupting the .


The breakthrough, published online in the journal PNAS this week (27 June), means long sections of DNA can be created quickly and efficiently by chemical methods.


DNA strands are widely used in biological and medical research, and clean and effective methods of making longer sections are of great value. Current techniques rely on the use of enzymes as biological catalysts. Joining DNA chemically is particularly interesting as it does not depend on enzymes so can be carried out on a large scale under a variety of conditions.


Co-author of the paper Tom Brown, Professor of at the University of Southampton, says: "We believe this is the first example of a chemical method of joining together longer strands of DNA that works well.


"Typically, synthesised DNA strands will be up to 150 bases; beyond that they are very difficult to make. We have doubled that to 300 and we can go further. We can also join together heavily modified , used in medical research for example, which normal enzymes might not want to couple together."


The Southampton team investigated whether the artificial links would be tolerated biologically within the bacteria E.coli.


"The genetic code could still be correctly read," says co-investigator Dr Ali Tavassoli.


"The artificial linkages act in stealth as they go undetected by the organism; the gene was functional despite containing 'scars' in its backbone. This opens up all sorts of possibilities."


The team is now hoping to secure funding to explore potential applications of the technology.


More information: The paper "Biocompatible artificial DNA linker that is read through by DNA polymerases and is functional in Escherichia coli" by Afaf H. El-Sagheer, A. Pia Sanzone, Rachel Gao, Ali Tavassoli and Tom Brown, of the University of Southampton, is published online by PNAS, 27 June 2011.


Provided by University of Southampton (news : web)

Hitting moving RNA drug targets

By accounting for the floppy, fickle nature of RNA, researchers at the University of Michigan and the University of California, Irvine have developed a new way to search for drugs that target this important molecule. Their work appears in the June 26 issue of Nature Chemical Biology.

Once thought to be a passive carrier of genetic information, RNA now is understood to perform a number of other vital roles in the cell, and its malfunction can lead to disease. The versatile molecule also is essential to retroviruses such as HIV, which have no DNA and instead rely on RNA to both transport and execute genetic instructions for everything the virus needs to invade and hijack its host. As more and more links to disease are discovered, the quest for drugs that target RNA is intensifying.

Searching for such drugs is not a simple matter, however. Most of today's drug-hunting tools are designed to find that bind to protein targets, but RNA is not a protein, and it differs from proteins in many key features. "So there's a growing need for high-throughput technologies that can identify compounds that bind RNA," said Hashim M. Al-Hashimi, the Robert L. Kuczkowski Professor of Chemistry and Professor of Biophysics at U-M.

Al-Hashimi and coworkers adapted an existing computational technique for virtually screening libraries of small molecules to determine their RNA-binding abilities. In this approach, the shape of a is first determined by or ; next, researchers run to compute how well various small molecules---potential drugs, for example---nestle into and bind to the target structure. RNA presents a major challenge to this methodology because it doesn't have just one configuration; it's a floppy molecule, and depending on which small molecule it binds, it can assume vastly different shapes.

It once was thought that encounters with actually caused RNA's shape changes, and that it was impossible to predict what shape an RNA would adopt upon binding to a given small molecule. However, in earlier research, Al-Hashimi's team challenged this conventional "induced-fit" concept by showing that the RNA, on its own, can dance through the various shapes that it adopts when bound to different drugs. The team discovered that each drug molecule simply "waits" for the RNA to morph into its preferred shape and then latches onto it.

The researchers' previous work involved creating "nano-movies" of RNA that capture this dance of shape changes. In this new study, the researchers froze individual "frames" from the nano-movies, each showing the RNA in a different conformation, and subjected each of them to virtual screening. To test the method in the "real world," they first tried it on compounds already known to bind a particular RNA molecule from HIV called TAR.

"We showed that by virtually screening multiple snapshots of TAR, we could predict at a useful level of accuracy how tightly these different compounds bind to TAR," Al-Hashimi said. "But if we used the conventional method and virtually screened a single TAR structure determined by X-ray crystallography or NMR spectroscopy, we failed to predict binding of these drugs that we know can bind TAR."

Next, the researchers tried using the method to discover new TAR-targeting drugs. They screened about 51,000 compounds from the U-M Life Sciences Institute's Center for Chemical Genomics. "From this relatively small compound library, we ended up identifying six new small molecules that bind TAR and block its interaction with other essential viral molecules," Al-Hashimi said.

What's more, one of the six compounds, netilmicin, showed a strong preference for TAR.

"Netilmicin specifically binds TAR but not other related RNAs," said former graduate student Andrew Stelzer. "We were very pleased with these results because one of the biggest challenges in RNA-targeted drug discovery is to be able to identify compounds that bind a specific RNA target without binding other RNAs. The ability of netilmicin to specifically bind TAR provides proof of concept for this new technology," said Stelzer.

Further experiments showed that, for the six potential drug molecules, the method not only successfully predicted that they would bind to TAR, it also showed---with atomic-level accuracy—where on the RNA molecule each drug would bind.

Al-Hashimi then turned the six drug candidates over to David Markovitz, a professor of infectious diseases at the U-M Medical School, who tested them in cultured human T cells infected with HIV. The point of this experiment was to see if the drugs would prevent HIV from making copies of itself, an essential step in the disease process.

"Netilmicin did in fact inhibit HIV replication," Markovitz said. "This result demonstrates that using an NMR spectrometer and some computers we can discover drugs that target RNA and are active in human cells."

In addition to testing compounds in existing molecular libraries, the virtual screening technique can be used to explore the potential of new compounds that have not yet been synthesized, Al-Hashimi said. "This opens up a whole new frontier for exploring RNA as a drug target and finding new compounds that specifically target it."

More information: Nature Chemical Biology: http://www.nature. … o/index.html

Provided by University of Michigan (news : web)

Zinc and the zebrafish: Fluorescent fish could hold the key to understanding diabetes

Scientists from Queen Mary, University of London have discovered a new way of detecting zinc in zebra fish, that could pave the way for furthering our understanding of diseases like type 2 diabetes, prostate cancer and Alzheimer's.

The results will be announced today (3 July) at the Sixth International Symposium on Macrocyclic and Supramolecular Chemistry, in Brighton.

Zinc is found throughout the body and involved in many that affect the function of the immune system and brain, reproduction, and . Zinc is also increasingly recognised as a key element in the treatment of a range of diseases, for example , and Alzheimer's disease.

It's unclear whether zinc is a cause of disease, or if it's employed to prevent its development or progression, and there is great interest in developing a which can detect zinc in the body. While a lot of work has been done in vitro, very few people have looked at how zinc works in whole organisms.

In this new study, Professor Mike Watkinson, Dr Stephen Goldup and Dr Caroline Brennan, from Queen Mary's School of Biological and , have focused their efforts on the development of a sensor for zinc to be used in studies on zebrafish (Danio rerio). Due to their fast development, can be grown outside the mother's body, and their embryos are transparent, allowing for a clear observation of their organs.

The team designed a sensor which switched on fluorescence in the fish when zinc was present. Professor Mike Watkinson explains:"Our probe is able to visualise zinc in various parts of the fish embryos, including the pancreas and we are excited that we can develop the technology further to help understand the role of zinc in the development of important disease like Type 2 Diabetes."

The team used a technique called 'click' chemistry, which is designed to generate substances quickly and reliably by joining small units together.

The sensor was found to be particularly sensitive to identifying zinc rather than other anions such as iron or copper, and it is hoped that with further development the technology can be used by other scientists working in these important fields.

More information: ‘Modular ‘click’ sensors for zinc and their application in vivo’ will be published in issue 47 of Chemical Communications.

Provided by Queen Mary, University of London (news : web)