Track 1: Applications of Mass Spectrometry

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). 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.

• Mass spectrometry in the pharmaceutical industry
• Polymers and Molecular Surfaces/Films
• Native Mass Spectrometry
• Antibody Mass Spectrometry
• Plasma Mass Spectrometry
• Mass Spectrometry in Drug Discovery
• Clinical application of mass spectrometry
• Chromatography Mass Spectrometry
• Protein Mass Spectrometry
• Market growth and new era of mass spectrometry
• Mass Spectrometry in petroleum, Space Science, astrobiology and atmospheric chemistry
• Mass spectrometry in food analysis, industry and environmental analysis
• Mass spectrometry in biology, Life Science and Biotechnology
• Mass Spectrometry in Metabolomics
• Mass spectrometry in polymer chemistry
• Structure Determination of Natural Products by Mass Spectrometry
• Mass Spectrometry using nano-optomechanical devices
• Organic and inorganic mass spectrometry
• Mass spectrometry in trace elements, trace gas and organic analysis
• Biomedical applications
• Proteomics and Immunoassay

Track 2: New Approaches in Mass Spectrometry

To validate the method, samples from two human embryos culture medium were analyzed by high-pressure liquid chromatography–mass spectrometry (HPLC–MS). 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.

• Protein phosphorylation and non covalent interaction
• Advances in isolation, enrichment and separation
• Structural proteomics and genomics
• Lipidomics, metabolomics and ultratrace analysis
• Nano scale and microfluidic separations
• Metabolomics/Lipidomics: new MS technologies
• Emerging separation technologies
• Hybrid Mass Spectrometry
• NMR Spectroscopy and NMR in biomedicine
• Approaches in glycoproteins and glycans
• MS Approaches in Carbohydrates ,microbes and biomolecule analysis
• Atom probe tomography
• Complementary Techniques and Multitechnique Approaches (XPS, GD-MS, …)

Track 3: Mass Spectrometry in Pharmaceutical Analysis

It is based on the conversion of the sample into ionized state, with or without fragmentation which are then identified by their mass-to-charge ratios (m/e). Mass spectroscopy provides rich elemental information, which is an important asset to interpret complex mixture components. Thus, it is an important tool for structure elucidation of unknown compounds. Mass spectroscopy also helps in quantitative elemental analysis, that is, the intensity of a mass spectra signal is directly proportional to the percentage of corresponding element.

• Atom probe tomography
• Protein phosphorylation and non covalent interaction
• Advances in isolation, enrichment and separation
• Structural proteomics and genomics
• Lipidomics, metabolomics and ultratrace analysis
• Nano scale and microfluidic separations

Track 4: Recent Advances and Development in 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.

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

Track 5: Mass Spectrometry in Proteome Research

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. 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.

• Mass spectrometry based proteomics
• Over expression and purification of the proteins
• Protein identification and validation
• Multidimensional protein identification technology – MudPIT
• Computational methods of mass spectrometry in proteomics
• Analysis of protein and proteome by mass spectrometry
• Mass spectrometry based quantitative proteomics
• Mass spectrometry data analysis in proteomics

Track 6: Mass Spectrometry in Polymer Chemistry

The excessive use of psychotropic substances, natural drugs, hallucinogens, and most recently “new psychoactive substances,” which are designed from skeletons of some natural drugs previously known, are the main focus of the development of new analytical methodologies, where mass spectrometry has had a key role. When a toxicological analysis needs to identify and quantify metabolites from unknown drugs, a screening can be performed by coupling different chromatography techniques, such as liquid and gas chromatography to mass spectrometry. The development of mass spectrometry methods has offered new possibilities for forensic toxicology analyses, where the identification and quantification of drugs of abuse are the most concerning issues in the forensic science. The prevalence of drug addiction and abuse in the population worldwide is significantly high, resulting in one of the main causes of high criminal activities .

Track 7: Fundamentals of 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).

• Instrumentation and method development
• MS dynamics and theory of gas phase ions
• Mass analyzer and Ionization source
• New ion activation methods in mass spectrometry
• Organic and inorganic mass spectrometry
• Protein sample and Charged peptide fragments
• Ambient and atmospheric pressure ionization
• Analytical method development

Track 8: Mass spectrometry imaging

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. 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). 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.

• Single-cell MALDI mass spectrometry imaging
• Biomolecular imaging mass spectrometry
• Quantitative imaging mass spectrometry
• Mass Spectrometry Imaging approaches and applications
• Secondary ion mass spectrometry (SIMS) Imaging

Track 9: Ionization Techniques

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.

• Field desorption and ionisation
• Nanospray ionisation
• Microelectronics
• Separation Techniques in Analytical Chemistry
• Ion Mobility Spectrometry
• Ionization techniques and Data processing
• Particle bombardment
• Gas Phase ionisation
• Matrix asisted laser desorption ionization
• Atmospheric pressure chemical ionization
• Electrospray ionization
• Positive or negative ionisation
• Ion Scattering (LEIS, MEIS, etc.)

Track 10: Mass spectrometry in Analytical Science

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).

• Analytical Chemistry in Industries
• Analytical Chemistry in Engineering
• Analytical Chemistry in Food Industries
• Analytical Chemistry in Immunology
• Instrumentation
• Relation between Analytical chemistry and Environmental Chemistry
• Importance of Analytical Chemistry in Pharmacy 

Track 11: Mass Spectrometry Configurations and Separation Techniques

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.

• Electron transfer dissociation mass spectrometry
• Micro/nanostructured materials
• Solid phase micro-extraction (SPME)
• Solid liquid separations and purification
• Liquid Liqiuid Extraction
• Design and demonstration of mass spectrometry
• Instrumentation principles involving mass spectrometry
• Mini/Portable/Fieldable mass spectrometry
• Time-of-flight mass spectrometry
• Proton-extraction-reaction mass spectrometry (PER-MS)
• Separation enhancement by electric means

Track 12: Chromatography and High Performance Liquid Chromatography (HPLC)

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.

• Developments in Liquid Chromatography and HPLC
• Molecular Exclusion Chromatography
• Ion Exchange Chromatography
• Partition Chromatography
• Adsorption Chromatography
• Chromatography applications and future aspects
• Instrumentation principles involving in Chromatography and HPLC
• Application of High Performance Liquid Chromatography (HPLC)
• Recent Novel Techniques in Chromatography
• Chromatography Industry and Market Analysis
• Separation Techniques in Analytical Chemistry
• Developments in ion chromatography
• Developments in Gas Chromatography
• Advances in Various Chromatographic Techniques
• Advances in HPLC and affinity chromatography
• HPLC Fingerprinting in Bioinformatics and Computational Biology

Track 13: Hyphenated Techniques (LC-NMR-MS, HPLC-ESI-MS, MC-ICP-MS, HPLC-ICP-MS, UPLC-Q-TOF/MS)

A Hyphenated technique is combination or coupling of two different analytical techniques with the help of proper interface. Hirschfield introduced the term “hyphenation” to refer to the on-line combination of a separation technique and one or more spectroscopic detection technique

• LC-NMR-MS
• HPLC-ESI-MS
• HPLC-CE-MS
• LA-ICP-MS
• MC-ICP-MS
• LC-MC-ICPMS
• FlFFF-ICP-MS
• HPLC-ICP-MS
• GC-ICP-MS

Track 14: Mass spectrometry in environmental analysis

Mass Spectrometry (MS) is a popular technique for environmental analysis because of its ability to carry out sensitive qualitative and quantitative analysis. A number of developments, particularly in the analyzers used to separate ions based on their mass-to-charge ratio, make it increasingly useful for environmental analysis. Analyzers vary depending on their mass measurement accuracy, resolving power, acquisition speed and linearity. Analyzers like time-of-flight and orbitrap have been investigated for environmental applications. Tandem MS using hybrid analyzers is further improving MS by using two rounds of mass analysis. It lends itself to environmental analysis because it is useful for analyzing analytes in complex mixtures, or with high sample matrix background. It has been used in pesticide analysis to identify compounds like nitrophenols, which are readily water soluble and can run-off into river water and make their way into drinking water supplies.

Track 15: Maintenance, Troubleshooting, Data Analysis and Experimentation in Mass Spectrometry

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.

• Data independent analysis, representation and acquisition
• General symptom and chromatographic symptom
• Temperature and pressure symptom
• Emerging Tools in Mass Spectrometry
• Safty and regulatory certification
• MSD hardware description
• Troubleshooting tips and tricks
• Hyper reaction monitoring

Track 16: Proteomics and its applications

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.

• Protein Biochemistry and Proteomics
• Proteomics in Computational and Systems Biology
• Plant Proteomics and Applications
• Food and Nutritional Proteomics
• Immunoproteomics and Clinical proteomics
• Protein Engineering and Molecular Design
• Neuroproteomics & Neurometabolomics
• Proteomics Technologies

Track 17: Spectroscopy

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.

• Mass Spectroscopy
• UV and IR spectroscopy
• X-ray spectrometry
• Ultrasonic correlation spectroscopy
• X-ray photoelectron spectrometry
• Ultraviolet-visible spectroscopy
• Infrared spectroscopy
• Nuclear magnetic resonance spectroscopy
• Molecular spectroscopy
• Ion Spectroscopy

Track 18 : Mass Spectrometry in Metabolomics and Lipidomics

A novel integrated metabolomics/lipidomics workflow is introduced enabling high coverage of polar metabolites and non-polar lipids within one analytical run. Dual HILIC and RP chromatography were combined to high-resolution mass spectrometry. As a major advantage, only one data file per sample was obtained by fully automated simultaneous analysis of two extracts per sample. Hence, the unprecedented high coverage without compromise on analytical throughput was not only obtained by the orthogonality of the chromatographic separations, but also by the implementation of dedicated sample preparation procedures resulting in optimum extraction efficiency for both sub-omes. Thus, the method addressed completely hydrophilic sugars and organic acids next to water-insoluble triglycerides.

Track 19: Nuclear Magnetic Resonance(NMR) Spectroscopy

Nuclear Magnetic Resonance (NMR) spectroscopy is an analytical chemistry technique used in quality control and reserach for determining the content and purity of a sample as well as its molecular structure. For example, NMR can quantitatively analyze mixtures containing known compounds. For unknown compounds, NMR can either be used to match against spectral libraries or to infer the basic structure directly. Once the basic structure is known, NMR can be used to determine molecular conformation in solution as well as studying physical properties at the molecular level such as conformational exchange, phase changes, solubility, and diffusion. In order to achieve the desired results, a variety of NMR techniques are available

Track 20: Clinical application of mass spectrometry

As mass spectrometric methods now offer a level of specificity and sensitivity unrealized by spectrophotometric- and immunoassay-based methods, mass spectrometry has entered the clinical laboratory where it is being used for a wide range of applications. In Clinical Applications of Mass Spectrometry: Methods and Protocols, expert researchers provide detailed step-by-step procedures for the analysis of number of analytes of clinical importance. This versatile and expansive volume covers mass spectrometry methods for analytes including a variety of drugs, hormones, and metabolic compounds spanning the disciplines of toxicology, therapeutic drug monitoring, endocrinology, and pediatric metabolism.

Track 21: UV, IR and Ion Spectroscopy

Ultraviolet–visible spectroscopy or ultraviolet–visible spectrophotometry (UV–Vis or UV/Vis) refers to absorption spectroscopy or reflectance spectroscopy in the ultraviolet and visible spectral regions. This means it uses light in the visible and adjacent ranges. The absorption or reflectance in the visible range directly affects the perceived color of the chemicals involved. In this region of the electromagnetic spectrum, atoms and molecules undergo electronic transitions. Absorption spectroscopy is complementary to fluorescence spectroscopy, in that fluorescence deals with transitions from the excited state to the ground state, while absorption measures transitions from the ground state to the excited state