Call for Abstract
5th International Conference on Current Trends in Mass Spectrometry and Chromatography, will be organized around the theme “Recent scientific innovatory approaches, novel technologies and applications of Mass Spectrometry and Chromatography”
Mass Spectrometry 2017 is comprised of 13 tracks and 112 sessions designed to offer comprehensive sessions that address current issues in Mass Spectrometry 2017.
Submit your abstract to any of the mentioned tracks. All related abstracts are accepted.
Register now for the conference by choosing an appropriate package suitable to you.
Mass spectrometry (MS) is an analytical technique that ionizes chemical species and separates the ions based on their mass to charge ratio. The new advancements in current trends of using mass spectrometry hold promises to address the shortcomings of data-dependent analysis and selected reaction monitoring (SRM) employed in shotgun and targeted proteomics, respectively the advancements includes all-ion fragmentation, Fourier transform-all reaction monitoring, SWATH Acquisition, multiplexed MS/MS, pseudo-SRM (pSRM) and parallel reaction monitoring (PRM).. Mass spectrometry in the analytical technique which is being used in laboratories by researches and scientist from past 25years.
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 1-1Metabolomics/Lipidomics: new MS technologies
- Track 1-2Nano scale and microfluidic separations
- Track 1-3Lipidomics, metabolomics and ultratrace analysis
- Track 1-4Structural proteomics and genomics
- Track 1-5Advances in isolation, enrichment and separation
- Track 1-6Protein phosphorylation and non covalent interaction
- Track 1-7Atom probe tomography
- Track 1-8MS Approaches in Carbohydrates ,microbes and biomolecule analysis
- Track 1-9Approaches in glycoproteins and glycans
- Track 1-10NMR Spectroscopy and NMR in biomedicine
- Track 1-11Hybrid Mass Spectrometry
- Track 2-1Forensic studies with Mass Spectrometry.
- Track 2-2Mass spectrometry in biology
- Track 2-3Mass Spectrometry in Drug Discovery
- Track 2-4Clinical application of mass spectrometry
- Track 2-5Mass spectrometry in polymer chemistry
- Track 2-6mass spectrometry in organic analysis
- Track 2-7Biomedical applications
- Track 2-8Proteomics and Immunoassay
- Track 2-9Structure Determination of Natural Products by Mass Spectrometry
- Track 2-10Mass Spectrometry using nano-optomechanical devices
- Track 2-11Plasma Mass Spectrometry
- Track 2-12Antibody Mass Spectrometry
- Track 2-13Native Mass Spectrometry
- Track 2-14Chromatography Mass Spectrometry
- Track 2-15Protein Mass Spectrometry
- Track 2-16Market growth and new era of mass spectrometry
- Track 2-17Mass Spectrometry in petroleum, Space Science, astrobiology and atmospheric chemistry
- Track 2-18 Mass spectrometry in food analysis, industry and environmental analysis
- Track 2-19Mass spectrometry in the pharmaceutical industry
It is indispensable tool for proteomics research. Mass spectrometry with proteome has given many advances in method of separation in proteomics, complete characterization of proteins have been the goal of proteomics
In recent the advancement of mass spectrometry gave lot of benefit to proteomics as mail tool. The study of proteins interactions by the intellectuals made the more easy by using the MS method in which they are getting accurate results for their tests.
The study gives the easy method of separation for complex protein peptides ionization techniques were made easier by mass spectrometry New mass spectrometers are still being developed, and existing designs continue to be improved by making them more sensitive, and by increasing their mass resolution, mass accuracy, stability, and scan speed.
New genomes are being sequenced, and new software packages are being developed to provide protein identifications with lower false-positive and false-negative rates. Computer systems and data storage systems capable of handling terabytes of data.
The advancements and the solutions of the challenges of proteomics with mass spectrometry will be delivered by the respected intellectuals in Mass spectrometry2017 conference.
- Track 3-1Proteomic and mass spectrometry technologies for biomarker discovery
- Track 3-2Applications of Proteomics
- Track 3-3Mass spectrometry coupled with Protein and peptide fraction
- Track 3-4Proteogenomics
- Track 3-5Separation methods for complex protein peptides
- Track 3-6Informatics for Peptidome Discovery
- Track 3-7Advances in mass spectrometry for lipidomics
- Track 3-8Protein Quantitation Using Mass Spectrometry in Drug Discovery
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 4-5Mass spectrometry for biomedical applications
- Track 4-6Physical and Biophysical Mass Spectrometry
- Track 4-7Triple Quadrupole GC-MS/MS, the next evolution
- Track 4-8Emerging Tools and Applications
Mass spectrometry imaging is a technique used in mass spectrometry to visualize the spatial distribution of chemical compositions e.g. compounds, biomarker, metabolites, peptides or proteins by their molecular masses. Although widely used traditional methodologies like radiochemistry and immunohistochemistry achieve the same goal as MSI, they are limited in their abilities to analyze multiple samples at once, and can prove to be lacking if researchers do not have prior knowledge of the samples being studied. Emergency Radiology in the field of MSI are MALDI imaging and secondary ion mass spectrometry imaging (SIMS imaging). Imaging Mass Spectrometry is a technology that combines advanced analytical techniques for the analysis of biomedical Chromatography with spatial fidelity. An effective approach for imaging biological specimens in this way utilizes Matrix-Assisted Laser Desorption Ionization Mass Spectrometry (MALDI MS). Briefly, molecules of interest are embedded in an organic matrix compound that assists in the desorption and ionization of compounds on irradiation with a UV laser. The mass-to-charge ratio of the ions are measured using a Tandem Mass Spectrometry over an ordered array of ablated spots. Multiple analytes are measured simultaneously, capturing a representation or profile of the biological state of the molecules in that sample at a specific location on the tissue surface.
- Track 5-1Single-cell MALDI mass spectrometry imaging
- Track 5-2Biomolecular imaging mass spectrometry
- Track 5-3Quantitative imaging mass spectrometry
- Track 5-4Mass Spectrometry Imaging approaches and applications
- Track 5-5Peptide Imaging Using Mass Spectrometry
As per principles 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 6-1Fundamentals, instrumentation and method development
- Track 6-2Ambient and atmospheric pressure ionization
- Track 6-3Analytical method development
- Track 6-4MS dynamics and theory of gas phase ions
- Track 6-5Ion spectroscopy
- Track 6-6New ion activation methods in mass spectrometry
- Track 6-7UV and IR spectroscopy
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 7-2Separation Techniques in Analytical Chemistry
- Track 7-3Positive or negative ionisation
- Track 7-4Electrospray ionization
- Track 7-5Atmospheric pressure chemical ionization
- Track 7-6Matrix asisted laser desorption ionization
- Track 7-7Gas Phase ionisation
- Track 7-8Field desorption and ionisation
- Track 7-9Particle bombardment
- Track 7-10Ionization techniques and Data processing
- Track 7-11Ion Mobility Spectrometry
- Track 7-12Current Trends in surface‐enhanced laser desorption/ionization‐time of flight‐mass spectrometry.
Mass Spectrometry Configurations and Techniques is regards to Mass Spectrometry configuration of source, analyzer, and detector becomes conventional in practice, often a compound acronym arises to designate it, and the compound acronym may be better known among nonspectrometrists than the component acronyms. The Mass Spectrometry instrument consists of three major components those are Ion Source: For producing gaseous ions from the substance being studied; Analyzer: For resolving the ions into their characteristics mass components according to their mass-to-charge ratio and Detector System: For detecting the ions and recording the relative abundance of each of the resolved ionic species. A Imaging Mass Spectrometry is simply a device designed to determine the mass of individual atoms or molecules. Atoms of different elements have different masses and thus knowledge of the molecular mass can very often be translated into knowledge of the chemical species involved. TOF MS is the abbreviation for Time of Flight Mass Spectrometry. Charged ions of various sizes are generated on the sample slide and MALDI is the abbreviation for "Matrix Assisted Laser Desorption/Ionization." Mass spectrometry consists basically of weighing ions in the gas phase. The instrument used could be considered as a sophisticated balance which determines with high precision the masses of individual atoms and molecules. Depending on the samples chemical and mechanical propertiess, different ionization techniques can be used. One of the main factor in choosing which ionization technique to be used is biochemical process. For samples that are not themolabile and relatively volatile, ionization such as Electron Impact and/or Chemical Ionization can be effectively used.
- Track 8-1UV and IR spectroscopy
- Track 8-2Electron transfer dissociation mass spectrometry
- Track 8-3Proton-extraction-reaction mass spectrometry (PER-MS)
- Track 8-4Time-of-flight mass spectrometry
- Track 8-5Mini/Portable/Fieldable mass spectrometry
- Track 8-6Instrumentation principles involving mass spectrometry
- Track 8-7Design and demonstration of mass spectrometry
- Track 8-8Liquid Liqiuid Extraction
- Track 8-9Solid liquid separations and purification
- Track 8-10Solid phase micro-extraction (SPME)
- Track 8-11Micro/nanostructured materials
- Track 8-12Separation 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 9-2Advances in HPLC and affinity chromatography
- Track 9-3Advances in Various Chromatographic Techniques
- Track 9-4Developments in Gas Chromatography
- Track 9-5Developments in ion chromatography
- Track 9-6Separation Techniques in Analytical Chemistry
- Track 9-7Chromatography Industry and Market Analysis
- Track 9-8Recent Novel Techniques in Chromatography
- Track 9-9Application of High Performance Liquid Chromatography (HPLC)
- Track 9-10Instrumentation principles involving in Chromatography and HPLC
- Track 9-11Chromatography applications and future aspects
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 10-1Data independent analysis, representation and acquisition
- Track 10-2General symptom and chromatographic symptom
- Track 10-3Temperature and pressure symptom
- Track 10-4Air leaks, contamination, error message
- Track 10-5Safty and regulatory certification
- Track 10-6MSD hardware description
- Track 10-7Troubleshooting tips and tricks
- Track 10-8Hyper reaction monitoring
Fragmentation is the dissociation of energetically unstable molecular ions formed from passing the molecules in the ionization chamber of a mass spectrometer. The fragments of a molecule is used to determine structural information of the molecule as it causes a pattern in the mass spectrum.
In organic Compounds When the vaporized organic sample passes into the ionization chamber of a mass spectrometer, it is bombarded by a stream of electrons. These electrons have a high enough energy to knock an electron off an organic molecule to form a positive ion. This ion is called the molecular ion - or sometimes the parent ion.
- Track 11-1Reactions in mass spectrometry fragmentation
- Track 11-2Fragmentation in organic compounds
- Track 12-1Innovations in chromatographic techniques
- Track 12-2HPLC in Biopharmaceutical data screening
- Track 12-3Principles of chromatography techniques
- Track 12-4LC-MS & GC-MS: Mass spectroscopy (MS) detection techniques coupled to chromatographic separations
- Track 12-5Pharmaceutical and Biomedical Applications of Chromatography techniques
Chromatography was used for separation of yellow and green plant pigments, Chromatography has since evolved into a very general separation method for many types of mixtures.Chromatographic methods are essential in the analytical and preparative separation of biological samples. Gel filtration chromatography (size exclusion chromatography) is often the method of choice to purify macromolecules, taking advantage of their different sizes and shapes. Ion exchange chromatography is also useful for the separation of macromolecules, operating based on the various net charges on their surface, which can be tuned via the pH of the medium. Biological specificity in enzyme-substrate, enzyme-inhibitor, receptor-ligand, antigen-antibody (and other) interactions is utilised in affinity chromatography. In this method, one interaction partner is immobilised on a solid surface (stationary phase) and can selectively bind its interacting partner from a mixture in the mobile phase. The other components of the mixture can then be removed by replacing the mobile phase (washing). The pure material is then eluted by applying a mobile phase that disrupts the specific interaction.
- Track 13-1Chromatographic bed shape techniques
- Track 13-2Physical state of mobile phase techniques of Chromatography
- Track 13-3Techniques by separation mechanism
- Track 13-4Special techniques