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3rd International Conference on Mass spectrometry, will be organized around the theme “Recent Advancement in Mass Spectrometry”
LCMS-2016 is comprised of 11 tracks and 61 sessions designed to offer comprehensive sessions that address current issues in LCMS-2016.
Submit your abstract to any of the mentioned tracks. All related abstracts are accepted.
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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 1-1Mass spectrometry in food science
- Track 1-2Metabolomics/Lipidomics: new MS technologies
- Track 1-3Structural proteomics and genomics
- Track 1-4Advances in isolation, enrichment and separation
- Track 1-5Approaches in glycoproteins and glycans
- Track 1-6Carbohydrates ,microbes and biomolecule analysis
- Track 1-7Protein phosphorylation and non covalent interaction
- Track 1-8Nano 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 2-1Mass Spectrometry as a Diagnostic and a Cancer Biomarker Discovery Tool
- Track 2-2Potential of metabolomics as a functional genomics tool
- Track 2-3Mass spectrometry and the age of the proteome
- Track 2-4Mass 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 3-1Types of Techniques used in Analytical Methodology
- Track 3-2Advanced Analytical Techniques
- Track 3-3Analytical Instrumentation
- Track 3-4Applications in Analytical Methods
- Track 3-5Analytical Methods in pharmaceutical Industries
- Track 3-6Validation 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 4-1Fundamentals, instrumentation and method development
- Track 4-2Single-cell MALDI mass spectrometry imaging
- Track 4-3Biomolecular imaging mass spectrometry
- Track 4-4Quantitative imaging mass spectrometry
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 5-3Advances in isolation, enrichment, derivatization and separation
- Track 5-4Microfluidics combined with mass spectrometry
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 6-1Ion spectroscopy
- Track 6-2New ion activation methods
- Track 6-3Ambient and atmospheric pressure ionization
- Track 6-4Analytical method development
- Track 6-5Reactions, dynamics and theory of gas phase ions
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 7-1Instrumentation principles,
- Track 7-2Design and demonstration
- Track 7-3Mini/Portable/Fieldable mass spectrometry
- Track 7-4Time-of-flight 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 8-1Electrospray ionization
- Track 8-2Atmospheric pressure chemical ionization
- Track 8-3Matrix asisted laser desorption ionization
- Track 8-4Gas Phase ionisation
- Track 8-5Field desorption and ionisation
- Track 8-6Particle bombardment
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
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 10-1Mass spectrometry in the pharmaceutical industry
- Track 10-2Ion Trap LC-MS
- Track 10-3Lipidomics, metabolomics and ultratrace analysis
- Track 10-4Mass spectrometry in polymer chemistry
- Track 10-5Geology- petroleum composition carbon dating
- Track 10-6Drug target discovery and validation
- Track 10-7Space Science, astrobiology and atmospheric chemistry
- Track 10-8Biomedical applications
- Track 10-9Clinical application of mass spectrometry
- Track 10-10Ion Trap LC-MS
Liquid chromatography in mass spectrometry is an analytical chemistry technique that combines the physical separation capabilities of liquid chromatography (or HPLC) with the mass analysis capabilities of mass spectrometry (MS). LC-MS is a powerful technique that has very high sensitivity, making it useful in many applications. Its application is oriented towards the separation, general detection and potential identification of chemicals of particular masses in the presence of other chemicals (i.e., in complex mixtures), e.g., natural products from natural-products extracts, and pure substances from mixtures of chemical intermediates. Preparative LC-MS systems can be used for rapid mass-directed purification of specific substances from such mixtures that are important in basic research, and pharmaceutical, agrochemical, food, and other industries
- Track 11-1Capillary electrophoresis-Mass spectrometry
- Track 11-2LCMS-software
- Track 11-3Clinical diagnostics in LCMS
- Track 11-4Protein purification & Protein fraction Analysis
- Track 11-5Applications of LC-MS