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In the Forefront of Research into Protein Folding and Macromolecular Complex Assembly
Date:12/4/2007

University of Leeds Publishes Results Acquired With Waters SYNAPT High

Definition MS System

MILFORD, Mass. and LEEDS, England, Dec. 4 /PRNewswire-FirstCall/ -- Waters Corporation (NYSE: WAT) announced today that the University of Leeds' Astbury Centre for Structural Molecular Biology has published the results of protein research conducted with its newly-acquired Waters(R) SYNAPT High Definition MS(TM) (HDMS) System in the Journal of the American Society of Mass Spectrometry (JASMS).

The SYNAPT(R) HDMS System is being used by the Ashcroft Laboratory to study the function of biological molecules. In an article appearing in the December 2007 issue of the JASMS, researchers at Leeds describe the successful separation and analysis of various folded forms of the proteins cytochrome c and beta-2-microglobulin, an achievement the Ashcroft Laboratory hopes will lead to a more complete understanding of the biological processes responsible for amyloid fibril formation, bacterial pilus aggregation and virus capsid assembly -- all associated with debilitating diseases.

Proteins are carefully folded, three-dimensional long-chain molecules assembled by the human body. When properly folded they regulate normal bodily functions. Several high profile diseases, including Alzheimer's, Creuzfeldt- Jakob's, and Parkinson's, can develop when certain proteins normally folded into a particular shape become misfolded, causing a chain of events that can lead to self-aggregation and amyloid fibril formation. Dr. Alison Ashcroft and her colleague Prof. Sheena Radford at the University of Leeds are studying one such protein, beta-2-microglobulin, to try to understand how it forms such fibrils which accumulate in the joints of dialysis patients and which are associated with dialysis-related amyloidosis. A detailed understanding of these processes at the molecular level will aid in the design of therapeutics.

New Form of Mass Spectrometry Giving New Dimensions to Biological Research

As a tool, conventional mass spectrometry is an excellent method for differentiating between proteins having different masses. However, as different conformers, or folded forms, of a particular protein have identical masses, it is virtually impossible to differentiate them by conventional means. That's where the Waters SYNAPT HDMS System, and its embedded ion mobility technology, has helped the University of Leeds.

"A protein can fold into a very compact 3-D structure or under certain conditions it can unfold into a more expanded structure. Even though these different 3-D structures have the same mass and mass-to-charge (m/z) ratio, the ion mobility capability of the SYNAPT HDMS System can separate them and tell you how much of the protein is in its folded form vs. the unfolded form. And as the cross-sectional areas of the two protein conformers are different, by being able to separate them by shape, the SYNAPT HDMS System allows us to distinguish between the various protein forms. The results are really amazing," says Dr. Alison Ashcroft, Reader in Biomolecular Mass Spectrometry and Mass Spectrometry Facility Manager.

The SYNAPT System from Waters has provided the lab with new insights into the assembly process. "It's adding a new dimension to our research. We can now quantify the amount of protein that is in its native state and the amount that is unfolded and partially folded. We can also monitor which particular conformers are consumed during the assembly process. This is providing important new insights and detail into how biomolecules work at the molecular level," adds Dr. Ashcroft.

Waters introduced the SYNAPT HDMS System at the American Society of Mass Spectrometry annual meeting in Seattle in June of 2006. It is the first commercially-available mass spectrometer with the ability to analyze ions by their size, shape and charge in addition to mass.

A Strategy for Managing Terabytes of Scientific Data

Given its complement of five different types of mass spectrometers, funded by the Biotechnology and Biological Sciences Research Council (BBSRC) and the Wellcome Trust, managing data is a huge challenge for The Ashcroft Laboratory. To manage data files more efficiently, the laboratory has chosen Waters NuGenesis Scientific Data Management System (SDMS).

"Backing up data daily to DVDs was getting out of hand. The SDMS takes data once a day from five mass spectrometers and backs it up automatically and our post-graduate students and post-docs can look at the data directly from their office computers. It's important we archive data because the government funding bodies request we store data for five or 10 years from the date it was created. Graduate students take four years to get their Ph.D., so they need the data accessible for four years or more, especially if they are writing papers after getting their Ph.D.," comments Ashcroft.

"People that aren't analytical chemists tend to think of a mass spectrometer as a sophisticated weighing machine. Often they don't realize that you can look at a protein's functionality and behaviour with the instrument and they can be quite surprised when they find out," says Ashcroft.

The full reference for Dr. Ashcroft's article in the Journal of the American Society of Mass Spectrometry is:

Monitoring co-populated conformational states during protein folding events using ESI-IMS-MS, D. P. Smith, K. Giles, R. H. Bateman, S. E. Radford, A. E Ashcroft, J. Am. Soc. Mass Spectrom., 2007 Dec; 18 (12): 2180 -- 90, DOI:10.1016/j.jasms.2007.09.017

Reprint requests should be addressed to A.E. Ashcroft, Astbury Centre for Structural Molecular Biology, Astbury Building, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT UK or email: a.e.ashcroft@leeds.ac.uk

About the Faculty of Biological Sciences at Leeds (http://www.fbs.leeds.ac.uk)

The University of Leeds' Faculty of Biological Sciences is one of the largest groups of life-science researchers within the UK, with nearly 150 academic staff and over 400 post-doctoral fellows and post-graduate students. The Faculty's current active research grant portfolio is around pounds Sterling 60M and funding organizations include charities, Research Councils, the European Union and industry. The Faculty has an outstanding research record and all major units of assessment were awarded Grade 5 in the last government (HEFCE) Research Assessment Exercise.

About the Astbury Centre at Leeds (http://www.astbury.leeds.ac.uk)

The Astbury Centre for Structural Molecular Biology is an interdisciplinary research centre of the University of Leeds. It was founded to carry out international quality research in all aspects of structural molecular biology. ACSMB brings together over fifty academic staff from various faculties of the University of Leeds who share common interests. It is named after W.T.Astbury, a biophysicist who laid many of the foundations of the field during a long research career at the University of Leeds (1928- 1961).

Dr Alison E Ashcroft (http://www.astbury.leeds.ac.uk/facil/mass.htm) is a Reader in Biomolecular Mass Spectrometry and Manager of the Mass Spectrometry Facility in the Astbury Centre for Structural Molecular Biology, Faculty of Biological Sciences, University of Leeds. Her research interests focus on the use and development of mass spectrometry to address biomolecular functionality.

Prof. Sheena E Radford (http://bmbsgi10.leeds.ac.uk) is Professor of Structural Molecular Biology in the Astbury Centre for Structural Biology, Faculty of Biological Sciences, University of Leeds. Her research interests focus on the mechanisms of protein folding, misfolding and assembly.

About Waters Corporation (http://www.waters.com)

Waters Corporation (NYSE: WAT) creates business advantages for laboratory- dependent organizations by delivering practical and sustainable innovation to enable significant advancements in such areas as healthcare delivery, environmental management, food safety, and water quality worldwide.

Pioneering a connected portfolio of separations science, laboratory information management, mass spectrometry and thermal analysis, Waters technology breakthroughs and laboratory solutions provide an enduring platform for customer success.

With revenue of $1.28 billion in 2006 and 4,700 employees, Waters is driving scientific discovery and operational excellence for customers worldwide.

The Biotechnology and Biological Sciences Research Council (BBSRC) (http://www.bbsrc.ac.uk) is the UK funding agency for research in the life sciences. Sponsored by Government, BBSRC annually invests ~380M pounds Sterling in a wide range of research that makes a significant contribution to the quality of life for UK citizens.

The Wellcome Trust (http://www.wellcome.ac.uk) is the largest charity in the UK. It funds innovative biomedical research in the UK and internationally, spending around pounds Sterling 500M each year.

Waters, SYNAPT, High Definition MS, High Definition Mass Spectrometry, NuGenesis and HDMS are trademarks of Waters Corporation.

Media Contact:

Brian J. Murphy

Waters Corporation

508-482-2614

Brian_J_Murphy@waters.com


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