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4th World Congress on Mass Spectrometry, will be organized around the theme “Recent advancements, novel applications and future approaches of Mass Spectrometry”

Euro Mass Spectrometry 2017 is comprised of keynote and speakers sessions on latest cutting edge research designed to offer comprehensive global discussions that address current issues in Euro Mass Spectrometry 2017

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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 1-1Mass spectrometry in the pharmaceutical industry
  • Track 1-2Native Mass Spectrometry
  • Track 1-3Chromatography Mass Spectrometry
  • Track 1-4Protein Mass Spectrometry
  • Track 1-5Market growth and new era of mass spectrometry
  • Track 1-6Mass Spectrometry in petroleum, Space Science, astrobiology and atmospheric chemistry
  • Track 1-7 Mass spectrometry in food analysis, industry and environmental analysis
  • Track 1-8Mass spectrometry in biology, Life Science and Biotechnology
  • Track 1-9Mass Spectrometry in Metabolomics
  • Track 1-10Antibody Mass Spectrometry
  • Track 1-11Plasma Mass Spectrometry
  • Track 1-12Mass Spectrometry in Drug Discovery
  • Track 1-13Clinical application of mass spectrometry
  • Track 1-14Mass spectrometry in polymer chemistry
  • Track 1-15mass spectrometry in trace elements, trace gas and organic analysis
  • Track 1-16Biomedical applications
  • Track 1-17Proteomics and Immunoassay
  • Track 1-18Structure Determination of Natural Products by Mass Spectrometry
  • Track 1-19Mass Spectrometry using nano-optomechanical devices
  • Track 1-20Polymers and Molecular Surfaces/Films

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 pseudospectrum), 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 2-1Metabolomics/Lipidomics: new MS technologies
  • Track 2-2Emerging separation technologies
  • Track 2-3Hybrid Mass Spectrometry
  • Track 2-4NMR Spectroscopy and NMR in biomedicine
  • Track 2-5Approaches in glycoproteins and glycans
  • Track 2-6MS Approaches in Carbohydrates ,microbes and biomolecule analysis
  • Track 2-7Atom probe tomography
  • Track 2-8Protein phosphorylation and non covalent interaction
  • Track 2-9Advances in isolation, enrichment and separation
  • Track 2-10Structural proteomics and genomics
  • Track 2-11Lipidomics, metabolomics and ultratrace analysis
  • Track 2-12Nano scale and microfluidic separations
  • Track 2-13Complementary Techniques and Multitechnique Approaches (XPS, GD-MS, ...)

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 3-1Advances in sample preparation and MS Interface design
  • Track 3-2Cs-SIMS,  MeV-SIMS , FIB-SIMS and In-situ liquid SIMS
  • Track 3-3TIMS and SSMS
  • Track 3-4MALDI-TOF, SELDI-TOF and TOF-SIMS
  • Track 3-5ICP-MS and IRMS
  • Track 3-6Accelerator Mass Spectrometry
  • Track 3-7Triple Quadrupole GC-MS/LC-MS, the next evolution
  • Track 3-8Physical and Biophysical Mass Spectrometry
  • Track 3-9Proteomic and mass spectrometry technologies for biomarker discovery
  • Track 3-10LC-MS & GC-MS: Mass spectroscopy (MS) detection techniques coupled to chromatographic separations
  • Track 3-11Advances in isolation, enrichment, derivatization and separation
  • Track 3-12Microfluidics combined with mass spectrometry
  • Track 3-13New developments in ionization and sampling
  • Track 3-14Ambient Mass Spectrometry (DESI, DICE, …etc)

Mass spectrometry (MS) - based proteomics allows the sensitive and accurate quantification of almost complete proteomes of complex biological fluids and tissues. At the moment, however, the routinely usage of MS-based proteomics is prevented and complicated by the very complex work flow comprising sample preparation, chromatography, MS measurement followed by data processing and evaluation. The new technologies, products and assays developed by Precision Proteomics could help enabling and establishing mass spectrometry (MS) - based proteomics in academic and pharmaceutical research as well as in clinical diagnostics.

  • Track 4-1Mass spectrometry based proteomics
  • Track 4-2Over expression and purification of the proteins
  • Track 4-3Protein identification and validation
  • Track 4-4Multidimensional protein identification technology – MudPIT
  • Track 4-5Computational methods of mass spectrometry in proteomics
  • Track 4-6Analysis of protein and proteome by mass spectrometry
  • Track 4-7Mass spectrometry based quantitative proteomics
  • Track 4-8Mass spectrometry data analysis in proteomics

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 5-1Instrumentation and method development
  • Track 5-2Ambient and atmospheric pressure ionization
  • Track 5-3Analytical method development
  • Track 5-4MS dynamics and theory of gas phase ions
  • Track 5-5Mass analyzer and Ionization source
  • Track 5-6New ion activation methods in mass spectrometry
  • Track 5-7Organic and inorganic mass spectrometry
  • Track 5-8Protein sample and Charged peptide fragments

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 6-1Single-cell MALDI mass spectrometry imaging
  • Track 6-2Biomolecular imaging mass spectrometry
  • Track 6-3Quantitative imaging mass spectrometry
  • Track 6-4Mass Spectrometry Imaging approaches and applications
  • Track 6-5Secondary ion mass spectrometry (SIMS) Imaging

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 7-1Nanospray ionisation
  • Track 7-2Microelectronics
  • Track 7-3Separation Techniques in Analytical Chemistry
  • Track 7-4Ion Mobility Spectrometry
  • Track 7-5Ionization techniques and Data processing
  • Track 7-6Particle bombardment
  • Track 7-7Field desorption and ionisation
  • Track 7-8Gas Phase ionisation
  • Track 7-9Matrix asisted laser desorption ionization
  • Track 7-10Atmospheric pressure chemical ionization
  • Track 7-11Electrospray ionization
  • Track 7-12Positive or negative ionisation
  • Track 7-13Ion Scattering (LEIS, MEIS, etc.)

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 8-1Electron transfer dissociation mass spectrometry
  • Track 8-2Micro/nanostructured materials
  • Track 8-3Solid phase micro-extraction (SPME)
  • Track 8-4Solid liquid separations and purification
  • Track 8-5Liquid Liqiuid Extraction
  • Track 8-6Design and demonstration of mass spectrometry
  • Track 8-7Instrumentation principles involving mass spectrometry
  • Track 8-8Mini/Portable/Fieldable mass spectrometry
  • Track 8-9Time-of-flight mass spectrometry
  • Track 8-10Proton-extraction-reaction mass spectrometry (PER-MS)
  • Track 8-11Separation enhancement by electric means

Liquid chromatography-mass spectrometry analysis of small molecules from biofluids requires sensitive and robust assays. Because of the very complex nature of many biological samples, efficient sample preparation protocols to remove unwanted components and to selectively extract the compounds of interest are an essential part of almost every bioanalytical workflow. 

High-performance liquid chromatography (HPLC) is a separation technique that can be used for the analysis of organic molecules and ions. HPLC is based on mechanisms of adsorption, partition and ion exchange, depending on the type of stationary phase used. HPLC involves a solid stationary phase, normally packed inside a stainless-steel column, and a liquid mobile phase. Separation of the components of a solution results from the difference in the relative distribution ratios of the solutes between the two phases. HPLC can be used to assess the purity and/or determine the content of many pharmaceutical bioprocessing substances. It can also be used to determine enantiomeric composition, using suitably modified mobile phases or chiral stationary phases. Individual separation mechanisms of adsorption, partition and ion exchange rarely occur in isolation since several principles act to a certain degree simultaneously.In a very environmental monitoring, hydrophilic molecules will tend to associate with each other (like water drops on an oily surface). The hydrophilic molecules in the mobile phase will tend to adsorb to the surface on the inside and outside of a particle if that surface is also hydrophilic. Increasing the polarity of the mobile phase will subsequently decrease the adsorption and ultimately cause the sample molecules to exit the column. This mechanism is called Normal Phase Analytical Chromatography. It is a very powerful technique that often requires non-polar solvents. Due to safety and environmental concerns this mode is used mostly as an analytical technique and not for process applications.

 

  • Track 9-1Developments in Liquid Chromatography and HPLC
  • Track 9-2Molecular Exclusion Chromatography
  • Track 9-3Ion Exchange Chromatography
  • Track 9-4Partition Chromatography
  • Track 9-5Adsorption Chromatography
  • Track 9-6Chromatography applications and future aspects
  • Track 9-7Instrumentation principles involving in Chromatography and HPLC
  • Track 9-8Application of High Performance Liquid Chromatography (HPLC)
  • Track 9-9Recent Novel Techniques in Chromatography
  • Track 9-10Chromatography Industry and Market Analysis
  • Track 9-11Separation Techniques in Analytical Chemistry
  • Track 9-12Developments in ion chromatography
  • Track 9-13Developments in Gas Chromatography
  • Track 9-14Advances in Various Chromatographic Techniques
  • Track 9-15Advances in HPLC and affinity chromatography
  • Track 9-16HPLC Fingerprinting in Bioinformatics and Computational Biology
  • Track 10-1LC-NMR-MS
  • Track 10-2 HPLC-ESI-MS
  • Track 10-3HPLC-CE-MS
  • Track 10-4 LA-ICP-MS
  • Track 10-5MC-ICP-MS
  • Track 10-6 LC-MC-ICPMS
  • Track 10-7FlFFF-ICP-MS
  • Track 10-8HPLC-ICP-MS
  • Track 10-9GC-ICP-MS

Mass spectrometry experiment (MS) is a high-throughput experimental method that characterizes molecules by their mass-to-charge ratio. The MS is composed of sample preparation, molecular ionization, detection, and instrumentation analysis processes. MS is beneficial in that it is generally fast, requires a small amount of sample, and provides high accuracy measurements. For these reasons, MS alone or combined with other structural proteomics techniques is widely used for various molecular biology analysis purposes. Examples of the analysis include post-translations modifications in proteins, identification of vibrational components in proteins, and analysis of protein conformation and dynamics. We will focus on MS-coupled methods that provide information about conformation and dynamics of the protein being studied. For a comprehensive review on MS procedures and for a review on various types of MS-coupled methods.The performance of a mass spectrometer will be severely impaired by the lack of a good vacuum in the ion transfer region of the mass analyser.  As the vacuum deteriorates it will become insufficient to maintain biomedical instrumentation in the operating mode. If the foreline pump is not maintained, the oil may become so contaminated that the  optimum pumping is no longer possible.  Initially, gas transport and metabolism ballasting may clean the oil.  If the  oil has become discoloured then it should be changed according to the pump  manufacturers’ maintenance manual.  When rotary pumps are used to pump away conflict resolution, the solvent can  become dissolved in the oil causing an increase in backing line pressure.  Gas  ballasting is a means of purging the oil to remove dissolved contaminants

  • Track 11-1Data independent analysis, representation and acquisition
  • Track 11-2General symptom and chromatographic symptom
  • Track 11-3Temperature and pressure symptom
  • Track 11-4Emerging Tools in Mass Spectrometry
  • Track 11-5Safty and regulatory certification
  • Track 11-6MSD hardware description
  • Track 11-7Troubleshooting tips and tricks
  • Track 11-8Hyper reaction monitoring

Proteomics has become an essential tool for understanding biological systems processes at the molecular level. Plant Proteomics publishes novel and significant research in the field of proteomics that examine the dynamics, functions, and interactions of proteins from plant systems. Nutritional proteomics is quickly developing to utilize little atom substance profiling to bolster incorporation of eating regimen and sustenance in complex biosystems research. Nutrigenomics is a branch of nutritional genomics and is the study of the effects of foods and food constituents on gene expression. Foodomics has been recently defined as a new discipline that studies food and nutrition domains through the application of advanced technologies in which MS techniques are considered indispensable. Applications of Foodomics include the genomic, transcriptomic, proteomic, and/or metabolomic study of foods for compound profiling, authenticity, and/or biomarker-detection related to food quality or safety; the development of new transgenic foods, food contaminants, and whole toxicity studies; new investigations on food bioactivity, food effects on human health. The University of Michigan Nutrition Obesity Research Center (UM NORC) started in 2010, supported by the National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK). The UM NORC is one of 12 U.S. focuses intended to move and backing translational, multi-disciplinary exploration in heftiness and sustenance, over the continuum of fundamental science to applications in people (solution) and populations (public health).

  • Track 12-1Protein Biochemistry and Proteomics
  • Track 12-2Proteomics in Computational and Systems Biology
  • Track 12-3Plant Proteomics and Applications
  • Track 12-4Food and Nutritional Proteomics
  • Track 12-5Immunoproteomics and Clinical proteomics
  • Track 12-6Protein Engineering and Molecular Design
  • Track 12-7Neuroproteomics & Neurometabolomics
  • Track 12-8Proteomics Technologies

Spectroscopy is the study of the interaction between matter and electromagnetic radiation. Historically, spectroscopy originated through the study of visible light dispersed according to its wavelength, by a prism. Later the concept was expanded greatly to include any interaction with radiative energy as a function of its wavelength or frequency. Spectroscopic data is often represented by an emission spectrum, a plot of the response of interest as a function of wavelength or frequency.

  • Track 13-1Mass Spectroscopy
  • Track 13-2UV and IR spectroscopy
  • Track 13-3X-ray spectrometry
  • Track 13-4Ultrasonic correlation spectroscopy
  • Track 13-5X-ray photoelectron spectrometry
  • Track 13-6Ultraviolet-visible spectroscopy
  • Track 13-7Infrared spectroscopy
  • Track 13-8Nuclear magnetic resonance spectroscopy
  • Track 13-9Molecular spectroscopy
  • Track 13-10Ion Spectroscopy