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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

The search of metabolites which are present in biological samples and the comparison between different samples allow the construction of certain biochemical patterns. The mass spectrometry (MS) methodology applied to the analysis of biological samples makes it possible for the identification of many metabolites. The 100 chromatograms were concatenated in a vector. This vector, which can be plotted as a continuous (2D pseudo spectrum),  greatly simplifies for one to understand the subsequent dimensional multivariate analysis. To validate the method, samples from two human embryos culture medium were analyzed by high-pressure liquid chromatography–mass spectrometry (HPLC–MS). They work on the principle that many microorganisms have their own unique mass spectral signature based on the particular proteins and peptides that are present in the cells. Identification of unknown peaks in gas chromatography (GC/MS)-based discovery metabolomics is challenging, and remains necessary to permit discovery of novel or unexpected metabolites that may allergic diseases  processes and/or further our understanding of how genotypes relate to phenotypes. Here, we introduce two new technologies and an advances in pharmaceutical analytical methods that can facilitate the identification of unknown peaks. First, we report on a GC/Quadrupole-Orbitrap mass spectrometer that provides high mass accuracy, high resolution, and high sensitivity analyte detection.

  • Track 2-1Mass spectrometry in food science
  • Track 2-2Metabolomics/Lipidomics: new MS technologies
  • Track 2-3Structural proteomics and genomics
  • Track 2-4Advances in isolation, enrichment and separation
  • Track 2-5Integrated OMICS in Mass spectrometry
  • Track 2-6Carbohydrates ,microbes and biomolecule analysis
  • Track 2-7 Nano scale and microfluidic separations

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

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 4-1Instrumentation principles
  • Track 4-2Design and demonstration
  • Track 4-3Mini/Portable/Fieldable mass spectrometry
  • Track 4-4Time-of-flight mass spectrometry
  • Track 4-5Electron transfer dissociation mass spectrometry
  • Track 4-6Separation enhancement by electric means
  • Track 4-7UV and IR spectroscopy
  • Track 4-8Micro/nanostructured materials
  • Track 4-9Solid Phase Micro-Extraction (SPME)
  • Track 4-10Solid liquid separations and purification
  • Track 4-11Liquid-Liquid Extraction

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 5-1Advances in sample preparation and MS Interface design
  • Track 5-2New developments in ionization and sampling
  • Track 5-3 Advances in isolation, enrichment, derivatization and separation
  • Track 5-4Microfluidics combined with mass spectrometry

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 6-1Types of Techniques used in Analytical Methodology
  • Track 6-2Advanced Analytical Techniques
  • Track 6-3Analytical Instrumentation
  • Track 6-4Applications in Analytical Methods
  • Track 6-5Analytical Methods in pharmaceutical Industries
  • Track 6-6Validation 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 7-1Fundamentals, instrumentation and method development
  • Track 7-2MALDI Imaging Mass Spectrometry
  • Track 7-3Single-cell MALDI mass spectrometry imaging
  • Track 7-4Biomolecular imaging mass spectrometry
  • Track 7-5Quantitative imaging mass spectrometry

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 8-1Atmospheric pressure chemical ionization
  • Track 8-2Matrix assisted laser desorption ionization
  • Track 8-3Gas Phase ionisation
  • Track 8-4Field desorption and ionisation
  • Track 8-5Particle bombardment
  • Track 8-6Electrospray ionization

Chromatography is one of several separation techniques defined as differential migration from a narrow initial zone. Electrophoresis is another member of this group. In this case, the driving force is an electric field, which exerts different forces on solutes of different ionic charge. The resistive force is the viscosity of the non-flowing solvent. The combination of these forces yields ion mobilities peculiar to each solute. Chromatography has numerous applications in biological and chemical fields. It is widely used in biochemical research for the separation and identification of chemical compounds of biological origin.In the petroleum industry the technique is employed to analyze complex mixtures of hydrocarbons.As a separation method, chromatography has a number of advantages over older techniques—crystallization, solvent extraction, and distillation, for example. It is capable of separating all the components of a multicomponent chemical mixture without requiring an extensive foreknowledge of the identity, number, or relative amounts of the substances present. It is versatile in that it can deal with molecular species ranging in size from viruses composed of millions of atoms to the smallest of all molecules—hydrogen—which contains only two; furthermore, it can be used with large or small amounts of material. Some forms of chromatography can detect substances present at the picogram (10−12 gram) level, thus making the method a superb trace analytical technique extensively used in the detection of chlorinated pesticides in biological materials and the environment, in forensic science, and in the detection of both therapeutic and abused drugs. Its resolving power is unequaled among separation methods.

  • Track 9-1Fundamentals of Chromatography
  • Track 9-2Types of Chromatography
  • Track 9-3Chromatography Software
  • Track 9-4Applications of Chromatography
  • Track 9-5Chromatography Solutions

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 10-1Selected reaction monitoring
  • Track 10-2Collision-induced dissociation
  • Track 10-3Electron-transfer dissociation
  • Track 10-4Infrared multiphoton dissociation
  • Track 10-5Electron capture dissociation
  • Track 10-6Blackbody infrared radiative dissociation
  • Track 10-7Electron-detachment dissociation
  • Track 10-8Surface-induced dissociation
  • Track 10-9Accelerator mass spectrometry

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 11-1Mass spectrometry in the pharmaceutical industry
  • Track 11-2Clinical application of mass spectrometry
  • Track 11-3Biomedical applications
  • Track 11-4Space Science, astrobiology and atmospheric chemistry
  • Track 11-5Drug target discovery and validation
  • Track 11-6Geology- petroleum composition carbon dating
  • Track 11-7Mass spectrometry in polymer chemistry
  • Track 11-8Lipidomics, metabolomics and ultratrace analysis
  • Track 11-9Ion Trap LC-MS

Creating ion source is the part of the mass spectrometer that ionizes the material under analysis (the analyte). The ions are then transported by magnetic or electric fields to the mass analyzer. Techniques for ionization have been key to determining what types of samples can be analyzed by mass spectrometry. Electron ionization and chemical ionization are used for gases and vapours. In chemical ionization sources, the analyte is ionized by chemical ion-molecule reactions during collisions in the source. Two techniques often used with liquid and solid biological samples include electrospray ionization and matrix-assisted laser desorption/ionization (MALDI, initially developed as a similar technique “Soft Laser Desorption” (SLD). Hard ionization and soft ionization, inductively coupled plasma and other ionization techniques are the sources for creating ions.

  • Track 12-1Hard ionization and soft ionization
  • Track 12-2Inductively coupled plasma
  • Track 12-3Other ionization techniques

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

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 14-1DMPK: Experimentation and Data Interpretation
  • Track 14-2High Resolution Mass Spectrometry for Qualitative and Quantitative Analysis

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 15-1LC-MS: Advanced Techniques and Applications
  • Track 15-2LC-MS: Practical Maintenance and Troubleshooting
  • Track 15-3LC/MS: The Techniques of Electrospray, APCI and APPI
  • Track 15-4HPLC Separations and Mass Analyzers
  • Track 15-5New Techniques: Chip Based Systems and direct analysis approaches

Metabolomics is an emerging field which combines strategies to identify and quantify cellular metabolites using sophisticated analytical technologies with the application of statistical and multi-variant methods for information extraction and data interpretation. Metabolomics is the study of small metabolites. Metabolomics Conference deals with topics like Bioinformatics, proteomics, systems biology, Analytical Techniques like NMR, GC-MS, LC-MS and CE-MS, Lipidomics, Metabolic Modelling, Metabolic profiling, clinical metabolomics, Translational sciences, Mass spectrometry, Metabolomics Syndrome, HPLC and CE based metabolomics and more.  Metabolomics - the new "omics" - is a dynamic and developing field, joining genomics, transcriptomics and proteomics in empowering an integrative frameworks science methodology to drug discovery and development. In spite of the fact that metabolomics is still at an early evolutionary stage it is conjecture that throughout the following decade the biopharma business will apply this innovation all the more generally in drug development and information.

  • Track 16-1New trends in mass spectrometry and medicine
  • Track 16-2Quantitation and structural elucidation of metabolites and covalent adducts
  • Track 16-3Challenges in Biopharmaceutical analysis
  • Track 16-4Novel high throughput techniques

This is an important branch of science because it provides many of the data that underlie policy decisions that can directly influence the health of people and ecosystems. Environmental mass spectrometry is currently undergoing rapid development. Among the most relevant directions are a significant broadening of the lists of formally targeted compounds; a parallel interest in nontarget chemicals; an increase in the reliability of analyses involving accurate mass measurements, tandem mass spectrometry, and isotopically labelled standards; and a shift toward faster high-throughput analysis, with minimal sample preparation, involving various approaches, including ambient ionization techniques and miniature instruments. A real revolution in analytical chemistry could be triggered with the appearance of robust, simple, and sensitive portable mass spectrometers that can utilize ambient ionization techniques. If the cost of such instruments is reduced to a reasonable level, mass spectrometers could become valuable household devices.

  • Track 17-1Ultra high resolution mass spectrometry and Petroleomics
  • Track 17-2Advanced Chromatographic Methods in Environmental Analysisy
  • Track 17-3Emerging and Persistent Environmental Contaminants
  • Track 17-4Novel applications in sampling and real time sample analysis by mass spectrometry I - Direct Analysis
  • Track 17-5Novel applications in sampling and real time sample analysis by mass spectrometry II - Continous, On-Line Monitoring
  • Track 17-6Environomics
  • Track 17-7Atomic MS in environmental applications

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 18-1Gaseous Biomolecules: Conformations, Energetics & Reactions
  • Track 18-2Biomolecular Structure: Covalent Labeling and Crosslinking
  • Track 18-3Gas phase ion chemistry and spectroscopy
  • Track 18-4Noncovalent Interactions: Proteins, Nucleic Acids, and Small Molecules
  • Track 18-5Biomolecular Structure: H,D-Exchange
  • Track 18-6AstroChemistry
  • Track 18-7Mass Spectrometric Insights into Catalysis
  • Track 18-8Protein-Protein Complexes