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6th Global Congress on Mass Spectrometry, will be organized around the theme “ Mass Spectrometry: Strategies and Technologies”
Mass Spectra 2017 is comprised of keynote and speakers sessions on latest cutting edge research designed to offer comprehensive global discussions that address current issues in Mass Spectra 2017
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As per Fundamentals of Mass Spectrometry, Mass spectrometry is an analytical tool used for measuring the molecular mass of a sample. Ionization is the atom or molecule is ionized by knocking one or more electrons off to give a positive ion. This is true even for things which you would normally expect to form negative ions or never form ions at all. Most mass spectrometers work with positive ions. New Ion activation methods for tandem mass spectrometry; this is followed by tandem mass spectrometry, which implies that the activation of ions is distinct from the laboratory research, and that the precursor and product ions are both characterized independently by their mass/charge ratios. As per the Frost and Sullivan report pharmaceutical analytical market is growing on an average 0.4% annually. This report studies the global mass spectrometry market over the forecast period of 2013 to 2018. Once analyte ions are formed in the gas phase, a variety of mass analyzers are available and used to separate the ions according to their mass-to-charge ratio (m/z). Mass spectrometers operate with the dynamics of charged particles in electric and magnetic particles in vacuum described by the Lorentz force law and Newton’s second law of motion
- Track 1-1Ion spectroscopy
- Track 1-2New ion activation methods
- Track 1-3Ambient and atmospheric pressure ionization
- Track 1-4Analytical method development
- Track 1-5Reactions, dynamics and theory of gas phase ions
There are many types of ionization techniques are used in mass spectrometry methods. The classic methods that most chemists are familiar with are electron impact (EI) and Fast Atom Bombardment (FAB). These techniques are not used much with modern mass spectrometry except EI for environmental work using GC-MS. Electrospray ionization (ESI) - ESI is the ionization technique that has become the most popular ionization technique. The electrospray is created by putting a high voltage on a flow of liquid at atmospheric pressure, sometimes this is assisted by a concurrent flow of gas. Atmospheric Pressure Chemical Ionization (APCI) - APCI is a method that is typically done using a similar source as ESI, but instead of putting a voltage on the Electrospray Tandem Mass Spectrometry Newborn Screening itself, the voltage is placed on a needle that creates a corona discharge at atmospheric pressures. Matrix Assisted Laser Electrophoresis is a technique of ionization in which the sample is bombarded with a laser. The sample is typically mixed with a matrix that absorbs the radiation biophysics and transfer a proton to the sample. Gas-Phase Ionization.
- Track 2-1Atmospheric pressure chemical ionization
- Track 2-2Matrix assisted laser desorption ionization
- Track 2-3Gas Phase ionisation
- Track 2-4Field desorption and ionisation
- Track 2-5Particle bombardment
- Track 2-6Electrospray ionization
Mass spectrometric analysis of biological samples has increasingly entailed direct analysis of complex protein mixtures, often with the objective of detailed characterization of the various components. This trend toward ever greater sample complexity has been enabled and in turn driven by the rapid development of powerful mass spectrometric tools. A general characteristic of recent mass spectrometers is that most are composed of a sequence of multiple mass analyzers with different strengths and properties, resulting in tandem instruments that possess capabilities unattainable by the individual components .can combine high mass accuracy with high-speed measurement, greatly facilitating the analysis of complex mixtures. This option is advantageous when speed and accuracy are crucial for the success of analysis, as it is, for example, when the mass spectrometer is coupled on-line to an HPLC system .Physical coupling of multiple mass spectrometers in tandem mass spectrometry has some disadvantages. Optimal operation conditions for different mass spectrometers and modes of operation of a tandem instrument may differ significantly, producing the need to compromise in the performance of one mass spectrometer at the expense of another Decoupling the parts of a hybrid instrument is one solution to this problem. The collected data can be analyzed quickly by a computer, which generates a set of instructions based on the results of analysis of the data obtained in the previous instrument and passes them to the next one. Theoretical speed of the analysis in such a modular tool is only limited by the speed of the sample analysis in the different instruments and the speed of transfer of the remaining part of the sample from one mass spectrometer to another. This concept has been used to combine a high resolution, high mass accuracy MALDI-QTOF instrument with a high-speed, high-sensitivity MALDI-IT mass spectrometer. This combination has proven to be extremely useful for gaining insight into many challenging biological problems Initial studies of the utility of this instrument combination utilized in-house modified instruments. However, the recent commercial introduction of similar mass spectrometers has opened the possibility to reproduce this approach in any laboratory.
- Track 3-1Mass Spectrometry as a Diagnostic and a Cancer Biomarker Discovery Tool
- Track 3-2Potential of metabolomics as a functional genomics tool
- Track 3-3Mass spectrometry and the age of the proteome
- Track 3-4 Mass spectrometry in proteomics
An analytical technique is a method that is used to determine the concentration of a chemical compound or chemical element. There are a wide variety of techniques used for analysis, from simple weighing (gravimetric analysis) to titrations (titrimetric) to very advanced techniques using highly specialized instrumentation. The most common techniques used in analytical chemistry are the following:Titrimetry, based on the quantity of reagent needed to react with the analyte,Electro analytical methods, including potentiometry and voltammetry.
Spectroscopy, based on the differential interaction of the analyte along with electromagnetic radiation,
Chromatography, in which the analyte is separated from the rest of the sample so that it may be measured without interference from other compounds;
There are many more techniques that have specialized applications, and within each major analytical technique there are many applications and variations of the general techniques.
- Track 4-1Types of Techniques used in Analytical Methodology
- Track 4-2Advanced Analytical Techniques
- Track 4-3Analytical Instrumentation
- Track 4-4Applications in Analytical Methods
- Track 4-5Analytical Methods in pharmaceutical Industries
- Track 4-6Validation of analytical Methods
Mass spectrometry imaging is a technique used in mass spectrometry to visualize the spatial distribution of chemical compositions e.g. compounds, biomarker, metabolites, peptides or proteins by their molecular masses. Although widely used traditional methodologies like radiochemistry and immunohistochemistry achieve the same goal as MSI, they are limited in their abilities to analyze multiple samples at once, and can prove to be lacking if researchers do not have prior knowledge of the samples being studied. Emergency Radiology in the field of MSI are MALDI imaging and secondary ion mass spectrometry imaging (SIMS imaging). Imaging Mass Spectrometry is a technology that combines advanced analytical techniques for the analysis of biomedical Chromatography with spatial fidelity. An effective approach for imaging biological specimens in this way utilizes Matrix-Assisted Laser Desorption Ionization Mass Spectrometry (MALDI MS). Briefly, molecules of interest are embedded in an organic matrix compound that assists in the desorption and ionization of compounds on irradiation with a UV laser. The mass-to-charge ratio of the ions are measured using a Tandem Mass Spectrometry over an ordered array of ablated spots. Multiple analytes are measured simultaneously, capturing a representation or profile of the biological state of the molecules in that sample at a specific location on the tissue surface.
- Track 5-1Fundamentals, instrumentation and method development
- Track 5-2MALDI Imaging Mass Spectrometry
- Track 5-3Single-cell MALDI mass spectrometry imaging
- Track 5-4Biomolecular imaging mass spectrometry
- Track 5-5Quantitative imaging mass spectrometry
Tandem mass spectrometry involves multiple steps of mass selection or analysis, usually separated by some form of fragmentation. A tandem mass spectrometer is one capable of multiple rounds of mass spectrometry. For example, one mass analyzer can isolate one peptide from many entering a mass spectrometer. A second mass analyzer then stabilizes the peptide ions while they collide with a gas, causing them to fragment by collision-induced dissociation (CID). A third mass analyzer then catalogues the fragments produced from the peptides. Tandem MS can also be done in a single mass analyzer over time as in a quadrupole ion trap. There are various methods for fragmenting molecules for tandem MS, including collision-induced dissociation (CID), electron capture dissociation (ECD), infrared multiphoton dissociation (IRMPD) and blackbody infrared radiative dissociation (BIRD).
- Track 6-1Selected reaction monitoring
- Track 6-2Collision-induced dissociation
- Track 6-3Electron-transfer dissociation
- Track 6-4Infrared multiphoton dissociation
- Track 6-5Electron capture dissociation
- Track 6-6Blackbody infrared radiative dissociation
- Track 6-7Electron-detachment dissociation
- Track 6-8Surface-induced dissociation
- Track 6-9Accelerator mass spectrometry
LC-MS is a key analytical chemistry technique that mixes the physical separation capabilities of liquid action with the mass analysis capabilities of mass spectroscopic analysis. LC-MS may be a powerful technique used for several applications that has terribly high sensitivity and property. Usually its application is destined towards the overall detection and potential identification of chemicals within the presence of alternative chemicals. LC-MS system is used for quick and mass directed purification of natural-products extracts and new molecular entities which are necessary to food, pharmaceutical, agrochemical and alternative industries.
- Track 7-1LC-MS: Advanced Techniques and Applications
- Track 7-2LC-MS: Practical Maintenance and Troubleshooting
- Track 7-3LC/MS: The Techniques of Electrospray, APCI and APPI
- Track 7-4HPLC Separations and Mass Analyzers
- Track 7-5New Techniques: Chip Based Systems and direct analysis approaches
New mass spectrometry (MS) methods, collectively known as data independent analysis and hyper reaction monitoring, have recently emerged. The analysis of peptides generated by proteolytic digestion of proteins, known as bottom-up proteomics, serves as the basis for many of the protein research undertaken by mass spectrometry (MS) laboratories. Discovery-based or shotgun proteomics employs data-dependent acquisition (DDA). Herein, a hybrid mass spectrometer first performs a survey scan, from which the peptide ions with the intensity above a predefined threshold value, are stochastically selected, isolated and sequenced by product ion scanning. n targeted proteomics, selected environmental Monitoring (ERM), also known as multiple reaction monitoring (MRM), is used to monitor a number of selected precursor-fragment transitions of the targeted amino acids. The selection of the SRM transitions is normally calculated on the basis of the data acquired previously by product ion scanning, repository data in the public databases or based on a series of empirical rules predicting the Enzyme structure sites.
- Track 8-1Advances in sample preparation and MS Interface design
- Track 8-2New developments in ionization and sampling
- Track 8-3 Advances in isolation, enrichment, derivatization and separation
- Track 8-4Microfluidics combined with mass spectrometry
Mass Spectrometry Configurations and Techniques is regards to Mass Spectrometry configuration of source, analyzer, and detector becomes conventional in practice, often a compound acronym arises to designate it, and the compound acronym may be better known among nonspectrometrists than the component acronyms. The Mass Spectrometry instrument consists of three major components those are Ion Source: For producing gaseous ions from the substance being studied; Analyzer: For resolving the ions into their characteristics mass components according to their mass-to-charge ratio and Detector System: For detecting the ions and recording the relative abundance of each of the resolved ionic species. A Imaging Mass Spectrometry is simply a device designed to determine the mass of individual atoms or molecules. Atoms of different elements have different masses and thus knowledge of the molecular mass can very often be translated into knowledge of the chemical species involved. TOF MS is the abbreviation for Time of Flight Mass Spectrometry. Charged ions of various sizes are generated on the sample slide and MALDI is the abbreviation for "Matrix Assisted Laser Desorption/Ionization." Mass spectrometry consists basically of weighing ions in the gas phase. The instrument used could be considered as a sophisticated balance which determines with high precision the masses of individual atoms and molecules. Depending on the samples chemical and mechanical propertiess, different ionization techniques can be used. One of the main factor in choosing which ionization technique to be used is biochemical process. For samples that are not themolabile and relatively volatile, ionization such as Electron Impact and/or Chemical Ionization can be effectively used.
- Track 9-1Instrumentation principles
- Track 9-2Design and demonstration
- Track 9-3Mini/Portable/Fieldable mass spectrometry
- Track 9-4Time-of-flight mass spectrometry
- Track 9-5Electron transfer dissociation mass spectrometry
- Track 9-6Separation enhancement by electric means
- Track 9-7UV and IR spectroscopy
- Track 9-8Micro/nanostructured materials
- Track 9-9Solid Phase Micro-Extraction (SPME)
- Track 9-10Solid liquid separations and purification
- Track 9-11Liquid-Liquid Extraction
Mass spectrometry (MS) is a mainstream chemical analysis technique in the twenty-first century. It has contributed to numerous discoveries in chemistry, physics and biochemistry. Hundreds of research laboratories scattered all over the world use MS every day to investigate fundamental phenomena on the molecular level. MS is also widely used by industry—especially in drug discovery, quality control and food safety protocols. In some cases, mass spectrometers are indispensable and irreplaceable by any other metrological tools. The uniqueness of MS is due to the fact that it enables direct identification of molecules based on the mass-to-charge ratios as well as fragmentation patterns. Thus, for several decades now, MS has been used in qualitative chemical analysis. To address the pressing need for quantitative molecular measurements, a number of laboratories focused on technological and methodological improvements that could render MS a fully quantitative metrological platform. In this theme issue, the experts working for some of those laboratories share their knowledge and enthusiasm about quantitative MS. I hope this theme issue will benefit readers, and foster fundamental and applied research based on quantitative MS measurements.
- Track 12-1DMPK: Experimentation and Data Interpretation
- Track 12-2High Resolution Mass Spectrometry for Qualitative and Quantitative Analysis
The MS-based detection of peptides and proteins in biological matrices can be divided in two main steps; they are sample clean-up and MS detection. The major challenges to detect growth promoting proteins and peptides are their generally low concentration, the complexity of the surrounding matrix, and the presence of endogenous proteins or isoforms. The complexity of the biological matrix requires highly specific clean-up procedures that are still compatible with the subsequent MS analysis. Common issues related to sample clean-up and MS detection approaches are, therefore, briefly summarized in the following section.
- Track 13-1Protein Structural Analysis by Mass Spectrometry
- Track 13-2Protein Therapeutics: Practical Characterization and Quantitation by Mass Spectrometry
- Track 13-3Radical Peptides
- Track 13-4Glycans and Glycoproteins in Mass Spectrometry
- Track 13-5Protein phosphorylation and non-covalent interaction
Application of Mass Spectrometry includes the ion and weights separation. The samples are usually introduced through a heated batch inlet, heated direct insertion probe, or a gas chromatograph. Ionization mass spectrometry (ESI-MS)which has become an increasingly important technique in the clinical laboratory for structural study or quantitative measurement of metabolites in a complex biological sample. MS/MS applications are plentiful, for example in elucidation of structure, determination of fragmentation mechanisms, determination of elementary compositions, applications to high-selectivity and high-sensitivity analysis, observation of ion–molecule reactions and thermochemical data determination (kinetic method).
Mass spectrometry is an analytical methods with high specificity and a growing presence in laboratory medicine. Various types of mass spectrometers are being used in an increasing number of clinical laboratories around the world, and, as a result, significant improvements in assay performance are occurring rapidly in areas such as toxicology, endocrinology, and biochemical markers. This review serves as a basic introduction to mass spectrometry, its uses, and associated challenges in the clinical laboratory and ends with a brief discussion of newer methods with the greatest potential for Clinical and Diagnostic Research.
- Track 14-1Mass spectrometry in the pharmaceutical industry
- Track 14-2Clinical application of mass spectrometry
- Track 14-3Biomedical applications
- Track 14-4Space Science, astrobiology and atmospheric chemistry
- Track 14-5Drug target discovery and validation
- Track 14-6Geology- petroleum composition carbon dating
- Track 14-7Mass spectrometry in polymer chemistry
- Track 14-8Lipidomics, metabolomics and ultratrace analysis
- Track 14-9Ion Trap LC-MS