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Germany and the UK but the Society has played its role in widening participation by involving the Dutch in Amsterdam (1988) and the Danes in Copenhagen (2006). The 2010 meeting is being held in Spain courtesy of the ‘turn’ of France but it is being recognised that widening participation even further is
long overdue. The Chromatographic Society hopes to be proactive in moving this process along. To touch again on Chris Bevan’s article on Eastern Europe, it is time for a bridge to be built between ISC and several satellite separation science symposium series in Eastern Europe through widening ISC to embrace Central and Eastern Europe (not to mention Scandinavia and Southern Europe) and more nations becoming actively involved in EuSSS. However, to get back to ISC 2010 (!), Valencia is a beautiful, historic venue which is still warm in September. More importantly, in fitting with one of the world,s major separation science meetings, the range of topics to be covered is exceptionally wide (Fundamentals of Chromatography, Gas Chromatography, Liquid Chromatography, Multidimensional
Chromatography, Hyphenated Techniques, Fast Separations, Column Technology, Electrodriven Separations, Supercritical Fluid Chromatography, Enantioseparations, New Detection Methods, Nanotechnology, Industrial and Process Chromatography, Environment
Speciation Analysis, Food quality and safety, Clinics and Pharmaceutics, Life Sciences / Bioanalysis, Forensics
Polymers (
http://isc2010.eu). The list of invited speakers in these topics is already looking impressive as well as multinational. Important dates are:
August 30, 2009 First Circular and Call for Papers April 15, 2010 Deadline for oral contributions June 30, 2010 Deadline for poster presentations
July 31, 2010 Deadline for last minute posters and early bird registration
September 12, 2010 Opening of ISC2010
If that were not enough, the Society will be rounding off its 2010 meetings calendar with another meeting at a major pharma venue. The actual venue for the meeting to be held in late October or early November is still to be confirmed but what is already certain is that the meeting topic will be “Biomacromolecules: the next big challenge for separation science” Some might argue that this is a challenge that is already upon us. Indeed, the Society held a meeting at Ware on a similar theme in November, 2008. However, with the increasing number of biologicals currently going through Pharmaceutical Development, it is a bi g and important challenge and revisiting the topic is more than justified.
Remember, you can get highly discounted members’ rates on these meetings by joining the Society. Top rate is £40 for Fellows. Students can join for a meagre £10! E-mail
chromsoc@meetingmakers.co.uk or call Matthew at Meeting Makers on 0141 434 1500
Wyatt Technology Corporation (USA) announces that Pfizer Global R&D, has chosen its DAWN®
(MALS) instrument to monitor protein reagent quality in drug discovery. The instrument’s unmatched analytical capabilities are illustrated in a new application note, titled “Using MALS to Ensure Protein Reagent Quality in Drug Discovery”, which is available to download free-of-charge via
www.wyatt.com
Quality and consistency of protein reagents are critical elements to successful drug discovery and development. When targeting a particular protein of interest, the best way to obtain dependable results is to perform different in vitro experiments using a protein with similar biological properties. It is important that molecularity, purity, shape and degree of heterogeneity remain the same regardless of any alterations of the model protein or the formulation buffer. Affinity tags or changes to buffer excipients may also be required.
Traditional characterization techniques, such as plate-based assays and biophysical methods where native proteins are preferred, are not efficient when alterations of solution properties of proteins occur. Crystallization studies, for example, typically have a higher
Protein Reagent Quality in Drug Discovery HELEOS®
Multi-Angle Light Scattering
rate of success when the proteins involved are simplified, whether they are truncated or expressed in bacteria to minimize post- translational modifications. MALS overcomes these limitations and has proven a very powerful technique for monitoring solution properties of proteins while changes to reagents are taking place.
The new application note demonstrates how light scattering data can be used to elucidate the solution properties of a protein expressed from two different constructs. The first construct was the shorter of the two, designed for crystallization studies. Experimental results, combined with the fact that the enzyme showed activity and was the predominant species in mass spectrometry, would lead to the erroneous confirmation of the suitability of the reagent. The DAWN HELEOS MALS data, however, showed that the enzyme was very heterogeneous. The second construct, which was designed to address this problem, was the full-length enzyme. In that case, the DAWN HELEOS demonstrated that the protein was in its biologically active form (dimer) and was highly homogenous. This information provided confidence to the project team at Pfizer to move forward with the second construct for crystallography, NMR and HTS studies.
For further information please email
wyatt@scottpr.com
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