5
The Posters were positioned in a single location in the Devonshire Park Hall that provided ample viewing space and time for discussions with poster presenters.
The meeting commenced with the Maccoll Lecture, honouring the memory of Alan Maccoll, a pioneer of mass spectrometry and a founding father of what is now the BMSS which was presented by Renato Zenobi from Department of Chemistry and Applied Biosciences, ETH Zurich, Switzerland. The lecture entitled ‘Exhalomics by Ambient Mass Spectrometry’ explained how exhaled breath contains important information on the state of a person’s health and that Mr Zenobi’s vision is to employ real-time non-invasive chemical analysis of exhaled breath for applications such as patient diagnosis, the treatment and monitoring of diseases, drug compliance/drug abuse, pharmacokinetics, and others. He proceeded to show in a very interesting lecture that the technique could be used in medical diagnosis, by showing examples of the detection of novel biomarkers for diseases such as obstructive sleep apnea (OSA) and chronic obstructive pulmonary disease (COPD). The methodology used to analyse breath in real time is based on secondary electrospray ionisation coupled to high-resolution mass spectrometry (SESI-HRMS) which provides ppb-ppt limits of detection for compounds with molecular weights up to 1000 Da.
His lecture was followed by the welcome mixer and exhibition, which was held in the Floral Hall.
The welcome mixer, enjoyed by all, consisted of red and white wine, nuts and crisps, a venerable feast for the starving Mass Spectrometrists and exhibitors who had been busy all day. Upon the conclusion those that were of a mind and still hungry left promptly at 20:00 for ‘The famous pub quiz’ which took place in the Horizon Suite at the View Hotel a short walk from the conference venue, with the incentive of ‘free chips’ for the fi rst 50 arrivals.
Figure 2. The 37th BMSS Annual Meeting Poster Session.
As usual, academia, industry and government were all well represented among the speakers and around 225 delegates were in attendance. The events were again accompanied by a one-and-a-half-day short course on the 12th and 13th September which was designed, in keeping with the societies mantra to have a more educational emphasis, for novices to mass spectrometry who wanted to gain a solid understanding of the instrumentation, and who wanted to gain an awareness of the vast fi eld of applications. For current mass spectrometry users, this provided an excellent refresher to the theory and a means to keep abreast of recent developments and advances in a rapidly changing fi eld.
Course Content
The course covered the fundamental aspects of mass spectrometry, assuming an undergraduate level of basic science, but required no previous practical experience or knowledge of the technique.
Attendees were introduced to the basic concepts and terminology of mass spectrometry and learned about the most important ionisation techniques used in mass spectrometry such as electron ionisation, a range of atmospheric pressure ionisation techniques, some of the more recent ambient ionisation/direct analysis techniques and matrix-assisted laser desorption/ ionisation. They also discovered how mass analysers work, including quadrupoles, ion traps, time-of-fl ight and Fourier transform mass spectrometers (Orbitrap and FT ICR), plus how hybrid mass spectrometers enable the design of the widest range of MS experiments to solve analytical problems: from compound characterisation to quantifi cation.
The BMSS Annual Meeting Conference
The aims of this BMSS annual meeting conference were to ‘of promoting knowledge and advancement in the fi eld of mass spectrometry, and providing a forum for the exchange of views and information’ and was opened with a brief welcome from the current chair Dr Christine Eckers. The format of the scientifi c programme this year was similar to that of previous meetings, with invited and contributed oral presentations and posters, but this year BMSS also decided to include keynote speakers for the sessions, designed to provide an in-depth view of their work.
Dr Jenny Ho - Full Characterisation of Heterogeneous Antibody Samples Under Denaturing and Native/Native-Like Conditions on a Hybrid Quadrupole-Orbitrap Mass Spectrometer.
The instrument and supplies exhibition, with a total of 27 vendors (four fewer than last year) covered the fl oor space available in The Floral Hall and created the ideal forum to assess the state-of-the-art of modern mass spec instrumentation with vendors having the opportunity to go into detail about their new products and developments.
The two-day meeting started in earnest on Wednesday with the Robinson Lecture, a lecture is a to recognise the contribution to Mass Spectrometry of Professor Carol Robinson. The lecture was titled ‘Protein Folding & Function: How Far Has Native MS Progressed?’ and was given by Professor Alison Ashcroft (University of Leeds).
Wednesday mornings two parallel sessions followed the plenary lecture and included the following oral presentations:
Session 1 - Glycomics
Chair: Professor David Harvey (University of Oxford)
Professor Anne Dell (ICL) - High Sensitivity Glycomics: Windows to Glycan Function
Radoslaw Kozak - Biopharmaceutical erythropoietin characterisation: critical quality attribute (CQA) mapping using LC-ESI- Qtof and automated database searching of glycopeptide and glycan analytes.
Anna Behrens - Site-specifi c N-glycan analysis of an HIV-1 Envelope trimer mimic.
Session 2 - Protein Complexes and Molecular Conformations
Chair: Professor Justin Benesch (University of Oxford)
Dr Kostas Thalassinos (UCL) - Combining mass spectrometry approaches for elucidating the structure and function of proteins containing large unstructured regions.
Heidi Gastall - Regulation of small Heat Shock Protein 27: Insights from Mass Spectrometry
Dr Adam Cryar - A Systematic Evaluation of the Integration of Ion Mobility into an Online Hydrogen Deuterium Exchange Mass Spectrometry Workfl ow
Aimee Paskins - Promotion and Manipulation of α-Synuclein Aggregation Observed Using ESI-IMS-MS
Two particularly interesting presentations were:
Firstly, Radoslaw P. Kozak (Ludger Ltd) discussed how glycosylation greatly infl uences the clinical performance and safety of recombinant erythropoietin (EPO) drugs and consequently how biopharma companies producing EPO products must carefully optimise, measure and control the glycosylation throughout the production lifetime of their drug. EPO contains 3 native N-link sites and a single O-link site but recombinant variants exist with more N-link sites added so EPO glycopeptide mapping is performed using a combination of an LC-ESI-QTof-MS instrument with a fl exible software program for glycopeptide characterisation which is populated with a user defi ned database of potential glycans. The LC methodology was also discussed using a wide pore nano C18 chromatography column. Another method described was EPO glycan characterisation using an N-glycan release and fl uorophore labelling strategy. This method used PNGase-F released procainamide labelled N-glycans which were separated using HILIC chromatography and detected by fl uorescence and ESI-MS/MS.
Figure 3. Christine Eckers opening the BMSS annual meeting. (Photo courtesy of BMSS)
Secondly Miss Aimee Paskins discussed how α-Synuclein is an intrinsically disordered, highly heterogeneous protein with no currently determined function and whose aggregation has been implicated in the pathogenesis of Parkinson’s disease. The proteins conformation and subsequent aggregation propensity are known to be altered as a response to its environment, and several factors have been identifi ed which increase or decrease the proteins aggregation rate. She utilised Electrospray Ionisation - Ion Mobility Spectrometry - Mass Spectrometry to demonstrate that the aggregation rate of the protein increased in the presence of metals via an increase in the more compact conformational states. This effect is further increased upon mimicking phosphorylation through amino acid substitutions at serine 87 and 129. We have determined the conformational changes
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