Evaporative sample preparation for mass spectrometry

Genevac has established a new web page that brings together customer technical articles that illustrate how centrifugal evaporation has become a sample preparation technique of choice for laboratories that seek to analyse complex samples using hyphenated mass spectrometry [MS] techniques. Many laboratories still rely upon the use of a rotary evaporator to perform the evaporation part of their sample preparation protocol prior to LC-MS or GC-MS analysis. While rotary evaporator methods often give good recoveries, they can only handle a single sample, require continuous monitoring to control the process and to ensure that no foaming or bumping occurs. For labs involved with GC-MS or LC-MS – Genevac SampleGenie™ technology in conjunction with a Rocket Synergy, HT or EZ-2 series evaporator is enabling large sample volumes to be dried directly into vials eliminating several time-consuming sample handling steps and the attendant risk of errors. SampleGenie is proven to reduce evaporation times by up to 66%, is compatible with a wide range of HPLC, GC and storage vial sizes and is a proven methodology for environmental analysis, metabolism and toxicology studies, food and beverage research, drugs of abuse testing as well as post purification protocols in life science research. Environmental analysis of persistent organic pollutants (POPs), glyphosphates and agal toxins are today a critical requirement in monitoring the quality of municipal water supplies. A paper is available for download that describes how a direct evaporative method developed to replace a solid phase extraction sample preparation technique that has traditionally been used prior to     LC-MS-MS analysis of algal toxins in lake water. The authors demonstrate how the direct evaporation sample preparation technique offers distinct advantages over solid phase extraction by eliminating the sample clean-up step, improving reproducibility, decreasing analysis time, minimising waste generation and being more cost effective.

MALDI-TOF Mass Spectrometry is a widely accepted technique for the elucidation and quantitation of biomolecules in life science research. However concentrating oligonucleotides, proteins, antibodies and other large biomolecules prior to analysis is not straightforward. A paper is available for download that describes how Genevac centrifugal evaporators have been able to protect these sensitive samples from thermal degradation and by preventing cross contamination between different samples in a microplate.

To review and download the ‘Evaporative Sample Preparation for Mass Spectrometry’ papers please visit www.evaporatorinfo.com/info24.html. For further information on centrifugal evaporators please visit www.genevac.com

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New controlled nucleation resource center

SP Scientific announces ControLyo^® Central, a new suite of online resources detailing how ControLyo^® Technology works and its benefits, as well as research publications and brochures. Central to the new resource center are a series of short video presentations assessing the implementation value of new freeze drying technologies to scientific cycle development, production environments, and for financial business impact to freeze dried parenterals manufacturers.  

Using an animated video format - SP Scientific introduces the science of ControLyo^® Technology, the process of implementation, and its potential financial benefits to businesses through factors such as shorter cycle times, reduced waste, and improved product quality. 

The video shows how staff at an illustrative pharmaceutical company are faced with slowed production due to lyophilization problems including variations in moisture levels, homogeneity and yield for a new injectable drug. The characters introduce ControLyo^® Technology and explain in simple terms how the technology affords precise control over the point of freezing during the lyophilization process - a critical factor affecting variability within a batch. Further they describe how ControLyo^® can reduce cycle time, virtually eliminate waste, improve product quality without requiring any formulation change and maintain sterility. Finally, the cost analysis demonstrates a typical 4-month payback on investment in ControLyo^® Technology in their production environment.

Additional videos within ControLyo^® Central include actual footage of traditional lyophilization vs. ControLyo^® Technology, and 'in action' applications involving lyophilization in both vials and syringes. Visitors to the site will find research publications and supporting literature with Spatially modulated illumination (SMI) microscopy images to further understand this innovative freeze drying breakthrough and its impact on product quality and production efficiencies. 

To watch these videos and learn more about ControLyo^® Technology please visit http://www.spscientific.com/ControLyo/. 

For further information please contact SP Scientific on +1-845-255-5000 / shireen.scott@spscientific.com

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Sample concentration prior to analysis

Genevac Rocket Synergy, HT and EZ-2 series evaporators are designed to be very useful tools for lab scientists wishing to concentrate a sample safely and quickly.

Genevac has remained an industry leader by partnering with customers to understand the obstacles involved in using centrifugal evaporation/concentration systems. This partnership has led to the development of a range of innovations including Dri-Pure^®, SampleGenie™, temperature control and highly solvent resistant build quality making Genevac evaporators the leading tools of choice for this concentration of samples prior to analysis.

Traditionally protocols for concentration of chromatographic fractions prior to analysis has involved drying multiple fractions in an evaporator, re-suspending pooled fractions into a single vial and then re-drying before storage and analysis. Even with modern centrifugal evaporators this process typically takes 2-3 days to complete. Now fractions can be pooled into a SampleGenie flask and dried directly into a submission vial in one evaporation run. SampleGenie is proven to reduce processing and evaporation times by up to 66% as well as eliminating the attendant risk of sample handling errors.  

SampleGuard and SampleShield temperature control are sample protection features included in all Genevac Rocket Synergy, HT and EZ-2 series evaporators. These proprietary technologies monitor and control the maximum temperature of the samples to protect them from any possibility of overheating when evaporation is complete. In addition, Genevac’s patented Dri-Pure^® sample protection system prevents cross-contamination and sample loss due to bumping and is fitted as standard on Rocket Synergy, HT and EZ-2 series evaporators.

For further information on safe and quick sample concentration prior to analysis please visit  evaporators please visit http://www.spscientific.com/ContentBlock.aspx?id=3505 or contact Genevac on +44-1473-240000 / +1-845-255-5000 / salesinfo@genevac.co.uk

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Graphene forged into three-dimensional shapes

Researchers from Finland and Taiwan have discovered how graphene, a single-atom-thin layer of carbon, can be forged into three-dimensional objects by using laser light. A striking illustration was provided when the researchers fabricated a pyramid with a height of 60 nm, which is about 200 times larger than the thickness of a graphene sheet. The pyramid was so small that it would easily fit on a single strand of hair. The research was supported by the Academy of Finland and the Ministry of Science and Technology of the Republic of China.

Graphene is a close relative to graphite, which consists of millions of layers of graphene and can be found in common pencil tips. After graphene was first isolated in 2004, researchers have learned to routinely produce and handle it. Graphene can be used to make electronic and optoelectronic devices, such as transistors, photodetectors and sensors. In future, we will probably see an increasing number of products containing graphene.

"We call this technique optical forging, since the process resembles forging metals into 3D shapes with a hammer. In our case, a laser beam is the hammer that forges graphene into 3D shapes," explains Professor Mika Pettersson, who led the experimental team at the Nanoscience Center of the University of Jyväskylä, Finland. "The beauty of the technique is that it's fast and easy to use; it doesn't require any additional chemicals or processing. Despite the simplicity of the technique, we were very surprised initially when we observed that the laser beam induced such substantial changes on graphene. It took a while to understand what was happening."

"At first, we were flabbergasted. The experimental data simply made no sense," says Dr Pekka Koskinen, who was responsible for the theory. "But gradually, by close interplay between experiments and computer simulations, the actuality of 3D shapes and their formation mechanism started to become clear."

"When we first examined the irradiated graphene, we were expecting to find traces of chemical species incorporated into the graphene, but we couldn't find any. After some more careful inspections, we concluded that it must be purely structural defects, rather than chemical doping, that are responsible for such dramatic changes on graphene," explains Associate Professor Wei Yen Woon from Taiwan, who led the experimental group that carried out X-ray photoelectron spectroscopy at the synchrotron facility.

The novel 3D graphene is stable and it has electronic and optical properties that differ from normal 2D graphene. Optically forged graphene can help in fabricating 3D architectures for graphene-based devices.

Source: Academy of Finland website

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Researchers have a new twist on asymmetric catalysis

In the same way a glove will only fit one hand, molecules have the symmetry that controls their behavior and interactions. In drug design, this means reversing the symmetry of a molecule can mean the difference between an effective treatment or a compound that has serious negative effects. As a further complication, making chemicals as a single pure mirror image, or separating mixtures of the two types, is very difficult.

Now a team of chemists of Osaka and Iwate Medical University has now developed a highly efficient way to make a unique screw-like chemical that could offer new routes to pure mirror images of other molecules. They reported their findings in Organic Letters.

"The twisted shape of helicenes makes them ideal for use in asymmetric catalysis" lead author Tetsuya Tsujihara says. "We previously developed a simple synthesis and resolution for this class of molecule and now, for the first time, we have added a thiophene group."

Helicene is a molecule with six hexagonal benzene molecules fused together so the rings twist back over themselves out of the plane of the molecule. The direction of the twist is locked, meaning two possible helices are possible, each a mirror image of the other. Think of the way a screw might turn clockwise or anticlockwise depending on the direction of the thread.

The researchers built upon their earlier studies, making and separating the two mirror images of helicene molecules. This time they changed their structure to include a new sulfur-containing group. This change could allow the screw-shaped molecules to be used as asymmetric catalysts for controlling interactions of other chemicals in reactions to directly produce molecules of a single mirror image.

"Adding the thiophene group is new development of the helicene skeleton, which should change the physical properties of the molecule and make these much more interesting to materials scientists," coauthor Tomikazu Kawano says. "We are also continuing to explore the promising asymmetric reactivity of these twisted catalysts."

Source: Osaka Univeristy website

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Mini-protein rapid design method opens way to create a new class of drugs

Scientists have created a high-speed method to generate thousands of different, small, stable proteins from scratch that can be custom-designed to bind to specific therapeutic targets.

Protection against infectious diseases, like the flu, and antidotes to nerve toxins are but two research goals of this approach.

These computer-designed proteins, which did not previous exist in nature, combine the stability and bioavailability of small molecule drugs with the specificity and potency of larger biologics.

"These mini-protein binders have the potential of becoming a new class of drugs that bridge the gap between small molecule drugs and biologics. They can be designed to bind to targets with high selectivity, but they are more stable and easier to produce and to administer," said David Baker professor of biochemistry at the University of Washington School of Medicine and director of the UW Institute for Protein Design, who led the multi-institutional research project.

Baker and his colleagues report their findings in article published online Sept. 27 by the journal Nature.

The method used a computer platform, called Rosetta, developed by Baker and colleagues at the University of Washington. They designed thousands of short proteins, about 40 amino acids in length, that the Rosetta program predicted would bind tightly to the molecular target.

Because of their small size, these short proteins tend to be extremely stable. They can be stored without refrigeration. They also are more easily administered than large protein drugs, such as monoclonal antibodies.

Previously, such short, protein-binder drugs were typically re-engineered versions of naturally occurring proteins. These, however, tended not to be significantly better than monoclonal antibodies.

Because these mini-proteins binders are original designs, they can be tailored to fit their targets much more tightly and are simpler to modify and refine.

The researchers sought to design two sets of these proteins: one set that would prevent the influenza virus from invading cells and another that would bind to and neutralize a deadly nerve toxin from botulism. This toxin is considered a potential bioweapon.

The computer modeling identified the amino-acid sequences of thousands of short proteins that would fit into and bind to the influenza and botulinum targets. The researchers created short pieces of DNA that coded each of these proteins, grew the proteins in yeast cells, and then looked at how tightly they bound to their targets. The targets were Influenza H1 hemagglutinin and botulinum neurotoxin B.

The method allowed them to design and test 22,660 proteins in a few months. More than than 2.000 of them bound to their targets with high affinity.

Evaluation of the best candidates found that the anti-influenza proteins neutralized viruses in cell culture and other designed proteins prevented the botulinum toxin from entering brain cells.

A nasal spray containing one of the custom-designed proteins completely protected mice from the flu if administered before or as much as 72 hours after exposure.. The protection that the treatment provides equaled or surpassed that seen with antibodies, the researchers report.

Testing of a subset of the proteins showed that they were extremely stable and, unlike antibodies, did not become inactivated by high temperatures. The small proteins also triggered little or no immune response, a problem that often renders larger protein drugs ineffective.

Source: NewsBeat UW Helath Sciences website