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7th World Congress on Mass Spectrometry, will be organized around the theme “Recent developments, applications and scientific research approaches of Mass Spectrometry”

Euro Mass Spectrometry 2018 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 2018

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

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 3-1Metabolomics/Lipidomics: new MS technologies
  • Track 3-2Nano scale and microfluidic separations
  • Track 3-3Lipidomics, metabolomics and ultratrace analysis
  • Track 3-4Structural proteomics and genomics
  • Track 3-5Advances in isolation, enrichment and separation
  • Track 3-6Protein phosphorylation and non covalent interaction
  • Track 3-7Atom probe tomography
  • Track 3-8MS Approaches in Carbohydrates ,microbes and biomolecule analysis
  • Track 3-9Approaches in glycoproteins and glycans
  • Track 3-10Hybrid Mass Spectrometry
  • Track 3-11Emerging separation technologies
  • Track 3-12Complementary 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 4-1Advances in sample preparation and MS Interface design
  • Track 4-2New developments in ionization and sampling
  • Track 4-3Microfluidics combined with mass spectrometry
  • Track 4-4Advances in isolation, enrichment, derivatization and separation
  • Track 4-5LC-MS & GC-MS: Mass spectroscopy (MS) detection techniques coupled to chromatographic separations
  • Track 4-6Proteomic and mass spectrometry technologies for biomarker discovery
  • Track 4-7Physical and Biophysical Mass Spectrometry
  • Track 4-8Triple Quadrupole GC-MS/LC-MS, the next evolution
  • Track 4-9Accelerator Mass Spectrometry
  • Track 4-10ICP-MS and IRMS
  • Track 4-12TIMS and SSMS
  • Track 4-13Cs-SIMS,  MeV-SIMS , FIB-SIMS and In-situ liquid SIMS
  • Track 4-14Ambient 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 5-1Mass spectrometry based proteomics
  • Track 5-2Over expression and purification of the proteins
  • Track 5-3Protein identification and validation
  • Track 5-4Multidimensional protein identification technology – MudPIT
  • Track 5-5Computational methods of mass spectrometry in proteomics
  • Track 5-6Analysis of protein and proteome by mass spectrometry
  • Track 5-7Mass spectrometry based quantitative proteomics
  • Track 5-8Mass spectrometry data analysis in proteomics

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

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 7-1Instrumentation and method development
  • Track 7-2Ambient and atmospheric pressure ionization
  • Track 7-3Analytical method development
  • Track 7-4MS dynamics and theory of gas phase ions
  • Track 7-5Mass analyzer and Ionization source
  • Track 7-6New ion activation methods in mass spectrometry
  • Track 7-7Organic and inorganic mass spectrometry
  • Track 7-8Protein 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 8-1Single-cell MALDI mass spectrometry imaging
  • Track 8-2Biomolecular imaging mass spectrometry
  • Track 8-3Quantitative imaging mass spectrometry
  • Track 8-4Mass Spectrometry Imaging approaches and applications
  • Track 8-5Secondary 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 9-1Nanospray ionisation
  • Track 9-2Positive or negative ionisation
  • Track 9-3Electrospray ionization
  • Track 9-4Atmospheric pressure chemical ionization
  • Track 9-5Matrix asisted laser desorption ionization
  • Track 9-6Gas Phase ionisation
  • Track 9-7Field desorption and ionisation
  • Track 9-8Particle bombardment
  • Track 9-9Ionization techniques and Data processing
  • Track 9-10Ion Mobility Spectrometry
  • Track 9-11Separation Techniques in Analytical Chemistry
  • Track 9-12Microelectronics
  • Track 9-13Ion Scattering (LEIS, MEIS, etc.)

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

The hyphenated technique is developed from the coupling of a separation technique and an on-line spectroscopic detection technology. The remarkable improvements in hyphenated analytical methods over the last two decades have significantly broadened their applications in the analysis of biomaterials, especially natural products. In this article, recent advances in the applications of various hyphenated techniques, e.g., GC-MS, LC-MS, LC-FTIR, LC-NMR, CE-MS, etc. in the context of pre-isolation analyses of crude extracts or fraction from various natural sources, isolation and on-line detection of natural products, chemotaxonomic studies, chemical fingerprinting, quality control of herbal products, dereplication of natural products, and metabolomic studies 

  • Track 11-1LC-NMR-MS
  • Track 11-2HPLC-ESI-MS
  • Track 11-3HPLC-CE-MS
  • Track 11-4 LA-ICP-MS
  • Track 11-5MC-ICP-MS
  • Track 11-6LC-MC-ICPMS
  • Track 11-7FlFFF-ICP-MS
  • Track 11-8HPLC-ICP-MS
  • Track 11-9GC-ICP-MS

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 12-1Mass Spectroscopy
  • Track 12-2Molecular spectroscopy
  • Track 12-3Nuclear magnetic resonance spectroscopy
  • Track 12-4Infrared spectroscopy
  • Track 12-5Ultraviolet-visible spectroscopy
  • Track 12-6X-ray photoelectron spectrometry
  • Track 12-7Ultrasonic correlation spectroscopy
  • Track 12-8X-ray spectrometry
  • Track 12-9UV and IR spectroscopy
  • Track 12-10Ion Spectroscopy

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 13-1Data independent analysis, representation and acquisition
  • Track 13-2General symptom and chromatographic symptom
  • Track 13-3Temperature and pressure symptom
  • Track 13-4Emerging Tools in Mass Spectrometry
  • Track 13-5Safty and regulatory certification
  • Track 13-6MSD hardware description
  • Track 13-7Troubleshooting tips and tricks
  • Track 13-8Hyper reaction monitoring