Track Categories

The track category is the heading under which your abstract will be reviewed and later published in the conference printed matters if accepted. During the submission process, you will be asked to select one track category for your abstract.

New mass spectrometry (MS) techniques, all things considered known as information free investigation and hyper response checking, have as of late developed. The investigation of peptides produced by photolytic assimilation of proteins, known as base up proteomics, fills in as the reason for a significant number of the protein explore attempted by mass spectrometry (MS) research facilities. Revelation based, or shotgun proteomics utilizes information subordinate obtaining (DDA). In this, a half and half mass spectrometer first play out a review check, from which the peptide particles with the power over a predefined limit esteem, are stochastically chosen, segregated and sequenced by item particle filtering. n focused on proteomics, chose natural Monitoring (ERM), otherwise called numerous response checking (MRM), is utilized to screen various chose antecedent part moves of the focused on amino acids. The choice of the SRM moves is regularly ascertained on the premise of the information obtained beforehand by item particle examining, store information in general society databases or in light of a progression of observational standards foreseeing the Enzyme structure destinations.

  • Track 1-1Microfluidics combined with Mass Spectrometry
  • Track 1-2Physical chemistry in Mass Spectrometry
  • Track 1-3Advances in sample preparation and MS Interface design
  • Track 1-4Advances in isolation, enrichment, derivatization and separation
  • Track 1-5Triple Quadrupole GC-MS/MS, the next evolution

Mass spectrometry is a very useful method for the determination of the structure of organic compounds although the technique has not yet been widely employed in this field. Of particular interest is the high sensitivity of the instrument, making possible the use of very small amounts of sample, and the information obtainable regarding the size of the molecule and position of the groups therein. 


Mass spectrometry is a analytical method used to quantify known materials, to determine unknown compounds within a sample, and to demonstrate the structure and chemical properties of different molecules. The complete process involves in the conversion of the sample into gaseous ions, with or without fragmentation, which are then characterized by their mass to charge ratios and relative abundances. Mass spectrometry technique basically studies the effect of ionizing energy on molecules. It depends upon chemical reactions in the gas phase in which sample molecules are consumed during the formation of ionic and neutral species.Mass spectrometry is  a powerful technique with a variable uses in biology, chemistry, and physics, but also in clinical medicine and even space exploration. It is used to determine the molecular weight of compounds by separating molecular ions on the basis of their mass and charge.

  • Track 3-1Mass spectrometry Uses in pharmaceutical industry
  • Track 3-2Tandem Mass Spectrometry
  • Track 3-3Mass Spectrometry Applications in Clinical Diagnostics
  • Track 3-4Mass spectrometry in Toxicology
  • Track 3-5Mass spectrometry and separation science in Biotechnology
  • Track 3-6Proteomics and its applications
  • Track 3-7Biochemical Applications of Mass Spectrometry in Drug Discovery
  • Track 3-8Mass Spectroscopy uses in forensic study
  • Track 3-9Organic Mass Spectrometry in Art and Archaeology
  • Track 3-10Capillary electrophoresis-Mass Spectrometry
  • Track 3-11Mass spectrometry in Pharmacognosy
  • Track 3-12Mass Spectrometry – Metabolomics
  • Track 3-13Ion-mobility separation Mass Spectrometry
  • Track 3-14Mass Spectrometry in Analytical chemistry
  • Track 3-15Mass spectrometry in Polymer Chemistry
  • Track 3-16Liquid chromatography–Mass Spectrometry (LC-MS)
  • Track 3-17Proton-Transfer-Reaction Mass Spectrometry (PTR-MS)
  • Track 3-18Mass spectrometry in organic chemistry

The use of Mass Spectrometry in the pharmaceutical region associated with the Drug Discovery and Development process is rich and varied. Many of the initial efforts were associated with online high performance liquid chromatography-mass spectrometry in drug  metabolismpharmacokinetic and pharmacodynamics studies. There have been numerous innovative efforts to apply various mass spectrometric techniques in early drug discovery, preclinical and clinical development, as well as in Phase 0 studies using Accelerator Mass Spectrometry. Today there is a re-evaluation and refocusing on how to efficiently adopt, adapt and use modern Mass Spectrometry instrumentation in the Drug Discovery and Development process.


  • Track 4-1Mass Spectroscopy uses in Drug metabolism
  • Track 4-2Mass Spectroscopy uses in Drug discovery
  • Track 4-3Mass Spectroscopy uses in combinatorial chemistry
  • Track 4-4Mass Spectroscopy Uses in Pharmacokinetics Study
  • Track 4-5Mass Spectroscopy Uses in Pharmacokinetics Study
  • Track 4-6Liquid Chromatography - Mass Spectrometry (LC-MS)
  • Track 4-7Liquid Chromatography - Mass Spectrometry (LC-MS)
  • Track 4-8Mass Spectroscopy Uses in pharmacodynamics study

Spectroscopy is the study of the interactions 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 5-1Mass Spectroscopy
  • Track 5-2UV and IR Spectroscopy
  • Track 5-3X-ray Spectrometry
  • Track 5-4Ultraviolet-visible Spectroscopy
  • Track 5-5Ion Spectroscopy
  • Track 5-6Nuclear Magnetic Resonance Spectroscopy
  • Track 5-7Infrared Spectroscopy
  • Track 5-8Molecular Spectroscopy

Clinical Laboratories utilizes the Mass spectrometry technology for disease screening, diagnosis of disease and metabolic disorders, identifying drug toxicity and poisoning, monitoring of drug therapy and determine advanced biomarkers. Therapeutic monitoring of immunosuppressant drugs using MS is well established. Liquid chromatography-mass spectrometry has become the standard for assay of steroid hormones for diagnosis of endocrine disorders. Vitamin D analysis by Liquid chromatography-mass spectrometry is widely used in the clinical laboratory today. Whereas immunoassays are unable to distinguish between 25-hydroxy vitamins D2 and D3, the Liquid chromatography-mass spectrometry methodologies are able to measure these levels separately so the contribution of each to the total can be determined. The capability of measuring thyroid hormones by tandem Mass spectrometry was developed recently and this has overcome the issues associated with immunoassays. Triple quadrupole MS/MS is the preferred methodology for toxicology screening and for toxic drug quantitation. In newborn and prenatal screening programs, electrospray tandem Mass spectrometry has made possible identification of inborn errors in metabolism or genetic defects so that preventive and medical intervention can be implemented promptly to relieve or treat. The intensive research into metabolomics, the assessment of endogenous metabolites as new disease biomarkers, is another promising applications of MS, which has been demonstrated to be very well suited to discovery and clinical application of metabolite profiles . Another area of increasing interest is the use of automated MALDI-TOF MS for rapid identification of microorganisms in clinical microbiology laboratories.


  • Track 6-1Mass Spectrometry uses in Neonatal Screening
  • Track 6-2Mass Spectrometry uses in hemoglobin analysis
  • Track 6-3Mass Spectrometry uses in Drug Testing
  • Track 6-4Plasma Mass Spectrometry

Capillary electrophoresis–mass spectrometry (CE-MS) is an analytical chemistry procedure formed by the combination of the liquid separation process of capillary electrophoresis with mass spectrometry. CE-MS combines advantages of both CE and MS to provide high separation efficiency and molecular mass information in a single analysis. It has high resolving power and sensitivity, requires minimal volume and can analyze at high speed. Ions are typically formed by electrospray ionization, but they can also be formed by matrix-assisted laser desorption/ionization or other ionization techniques. It has applications in basic research in proteomics and quantitative analysis of biomolecules as well as in clinical medicine.


  • Track 7-1Capillary Electrophoresis - MS of lipopolysaccharides
  • Track 7-2Capillary Electrophoresis-Mass Spectrometry of glucose ladders
  • Track 7-3Capillary Electrophoresis - MS of N-glycan
  • Track 7-4Matrix-assisted laser desorption/ionization
  • Track 7-5Electrospray ionization
  • Track 7-6Capillary Electrophoresis - MS for the analysis of intact Proteins
  • Track 7-7Capillary Electrophoresis-Mass Spectrometry of Glycopeptides
  • Track 7-8Capillary Electrophoresis-MS determination of sialic acids

Liquid chromatography-Mass spectrometry is a analytical chemistry process that mixes the physical separation capabilities of liquid action with the mass analysis capabilities of mass analysis. Liquid chromatography-Mass spectrometry  may be a powerful technique used for several applications that has terribly high sensitivity and property. Usually its application is destined towards the overall detection and potential identification of chemicals within the presence of alternative chemicals. LC-MS system is used for quick and mass directed purification of natural-products extracts and new molecular entities which are necessary to food, pharmaceuticalagrochemical and alternative industries.

Gas chromatography–mass spectrometry (GC-MS) is an analytical method that combines the features of gas-chromatography and mass spectrometry to identify different substances within a test sample. Applications of GC-MS include drug detection, fire investigation, environmental analysisexplosives investigation, and identification of unknown samples, including that of material samples obtained from planet Mars during probe missions as early as the 1970s. GC-MS can also be used in airport security to detect substances in luggage or on human beings. Additionally, it can identify trace elements in materials that were previously thought to have disintegrated beyond identification.


  • Track 8-1Advanced Techniques and Applications of HPLC
  • Track 8-2Practical Maintenance and Troubleshooting of HPLC
  • Track 8-3HPLC Separations and Mass Analyzers
  • Track 8-4Partition Chromatography
  • Track 8-5Gas chromatography
  • Track 8-6Gas chromatography detectors
  • Track 8-7Recent Novel Techniques in Chromatography
  • Track 8-8Recent Novel Techniques in Chromatography
  • Track 8-9Ion Exchange Chromatography
  • Track 8-10Adsorption Chromatography
  • Track 8-11Chromatography Industry and Market Analysis
  • Track 8-12Quadrupole Mass Analyzer
  • Track 8-13Quadrupole Mass Analyzer
  • Track 8-14Liquid Chromatography - Mass Spectrometry
  • Track 8-15High Resolution Mass Spectrometry

Tandem mass spectrometry explains various steps of mass selection or analysis, usually separated by some form of fragmentation. In a tandem mass spectrometer, ions are formed in the ion source and separated by mass-to-charge ratio in the first stage of mass spectrometry (MS1). Ions of a particular mass-to-charge ratio (precursor ions) are selected and fragment ions (product ions) are created by collision-induced dissociationion-molecule reactionphoto dissociation, or other process. The resulting ions are then separated and detected in a second stage of mass spectrometry (MS2). There are different methods for fragmenting molecules for tandem MS, including electron capture dissociation (ECD), collision-induced dissociation (CID), blackbody infrared irradiative dissociation (BIRD) and infrared multi photon dissociation (IRMPD).


  • Track 9-1Time-of-Flight Mass Spectrometry
  • Track 9-2Collision-induced dissociation
  • Track 9-3Electron-transfer dissociation
  • Track 9-4Electron-transfer dissociation
  • Track 9-5Infrared multiphoton dissociation
  • Track 9-6Electron capture dissociation
  • Track 9-7Blackbody infrared radiative dissociation
  • Track 9-8Electron-detachment dissociation
  • Track 9-9Electrospray Tandem Mass Spectrometry Newborn Screening
  • Track 9-10Newborn Screening by Tandem Mass Spectrometry

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 orbit rap 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 nitro phenols, which are readily water soluble and can run-off into river water and make their way into drinking water supplies.


  • Track 10-1Mass Spectroscopy used analysis of water quality
  • Track 10-2Determination of Polycyclic Aromatic Hydrocarbons in Seafood
  • Track 10-3Determination of Polychlorinated Biphenyls
  • Track 10-4Mass spectrometry for determining food contamination

Protein mass spectrometry refers to the uses of mass spectrometry to the study of proteins. Mass spectrometry is an important method for the accurate mass determination and characterization of proteins, and a variety of methods and instrumentations have been developed for its many uses. Its applications include the identification of proteins and their post-translational modifications, the elucidation of protein complexes, their subunits and functional interactions, as well as the global measurement of proteins in proteomics. It can also be used to localize proteins to the various organelles, and determine the interactions between different proteins as well as with membrane lipids. The two primary methods used for the ionization of protein in mass spectrometry are electrospray ionization (ESI) and matrix-assisted laser desorption/ionization.


  • Track 11-1Deuterium exchange Mass Spectrometry
  • Track 11-2Protein identification
  • Track 11-3Protein structure determination
  • Track 11-4Protein quantitation
  • Track 11-5Electrospray ionization
  • Track 11-6Matrix-assisted laser desorption/ionization
  • Track 11-7Matrix-assisted laser desorption/ionization
  • Track 11-8Biomarkers
  • Track 11-9Protein folding by Mass spectrometry
  • Track 11-10Proteomics and its Applications

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 12-1Field desorption and Ionization
  • Track 12-2Particle bombardment
  • Track 12-3Separation Techniques in Analytical Chemistry
  • Track 12-4Ion Mobility Spectrometry
  • Track 12-5Ionization techniques and Data processing
  • Track 12-6Matrix asisted laser desorption ionization
  • Track 12-7Atmospheric pressure chemical ionization
  • Track 12-8Quadrupole Mass Analyzer
  • Track 12-9Gas Phase Ionization

Mass Spectrometer generates multiple ions from the sample under investigation, it then separates them according to their specific mass-to-charge ratio (m/z), and then records the relative abundance of each ion type. The instrument consists of three major components. Ion Source, Analyzer, Detector System. A Mass Spectrometer should always perform the following processes:

Produce ions from the sample in the ionization source Separate these ions according to their mass-to-charge ratio in the mass analyzer          Eventually, fragment the selected ions and analyze the fragments in a second analyzer Detect the ions emerging from the last analyzer and measure their abundance with the detector that converts the ions into electrical signals Process the signals from the detector that are transmitted to the computer and control the instrument using feedback


Mass spectrometry in forensic analysis is a technology provides a powerful tool for forensic studies. For forensic researchers investigating their samples for unknown compounds, drug metabolites, chemicals or hazards, novel psychoactive substances that have never been previously detected or characterized. The role of mass spectroscopy in forensic science may be characterized as either molecular or elemental analysis. comparatively little volatile nonionic molecules found in a very sort of forensic samples may be analyzed with electron and chemical ionization of single-stage mass analyzers that give relative molecular mass and structural data. Non-polar and polar molecules and their metabolites habitually found in biological matrices along with alternative analytes of forensic interest may be determined by using electrospray.


  • Track 14-1Mass Spectrometry in Toxicology
  • Track 14-2Mass spectrometry uses in Explosive residue
  • Track 14-3Mass spectrometry uses in arson investigation
  • Track 14-4Mass spectroscopy uses in trace evidence

Mass spectrometry in medicine is the most important area to study for the development of medicines. Mass spectrometry is an analytic technique widely used many laboratories for the development of laboratory medicine. Various types of mass spectrometers are used in order to get improvements in assay performance that is occurring rapidly in areas such as toxicologyendocrinology, and biochemical genetics. Mass spectrometry is a diagnostic system with high specificity and developing vicinity in research facility prescription. Different sorts of mass spectrometers are being utilized as a part of an expanding number of clinical research facilities around the globe. Mass spectrometry has contributed altogether to the development of restorative science in late decades, especially in connection to medication advancement, in-vitro diagnostics, dietary and natural drug.


  • Track 15-1Mass Spectrometry and Illicit Drug Testing
  • Track 15-2Gangliosides and Mass Spectrometry
  • Track 15-3Mass Spectrometry - Metabolomics
  • Track 15-4Mass Spectrometry- Clinical Biomarker Discovery
  • Track 15-5Tandem Mass Spectrometry in Newborn Screening

Imaging Mass Spectrometry is a technology that combines most advanced analytical techniques for the analysis of biological molecules with spatial fidelity. An effective approach for imaging biological specimens in this way utilizes Matrix-Assisted Laser Desorption Ionization Mass Spectrometry. The mass-to-charge ratio  of the ions are measured using a Mass Spectrometer over an ordered array of ablated spots. Imaging Mass spectrum analysis (IMS) encompasses a spread of techniques that change the chemical imaging of analytes from atoms and little molecules to intact proteins directly from biological tissues. Imaging Mass Spectrometry is remodeling specific areas in research project with its distinctive combination of chemical and biological information. Innovations in instrumentation and imaging protocols can create this approach at several stages of the drug discovery method, as well as medical target screening and evaluating the distribution of drug and drug metabolites in cells and tissues.


  • Track 16-1Matrix-Assisted Laser Desorption/Ionization
  • Track 16-2Matrix-Assisted Laser Desorption/Ionization
  • Track 16-3Desorption Electrospray Ionization
  • Track 16-4laser ablation Electrospray Ionization
  • Track 16-5Nanospray Desorption Electrospray Ionization

Analytical Chemistry is the science of obtaining, processing, and communicating information about the composition and structure of matter. Analytical chemistry studies and uses instruments and methods used to separate, identify, and quantify matter.  In practice separation, identification or quantification may constitute the entire analysis or be combined with another method. Separation isolates analytes. Qualitative analysis identifies analytes, while Quantitative analysis determines the numerical amount or concentration. Analytical chemistry consists of classical, wet chemical methods and modern, instrumental methods. Classical qualitative methods use separations such as precipitation, extraction and distillation. Identification may be based on differences in color, odor, melting point, boiling point, radioactivity or reactivity. Classical quantitative analysis uses mass or volume changes to quantify amount. Instrumental methods may be used to separate samples using EhromatographyElectrophoresis or field flow fractionation. Then Qualitative and Quantitative analysis can be performed, often with the same instrument and may use light interaction, heat interaction, electric fields or magnetic fields . Often the same instrument can separate, identify and quantify an analyte. Analytical chemistry is also focused on improvements in experimental design, chemo metrics, and the creation of new measurement tools. Analytical chemistry has broad applications to forensics, medicine, science and engineering.


  • Track 17-1Proton-Transfer-Reaction Mass Spectrometry (PTR-MS)
  • Track 17-2Rutherford backscattering Spectrometry
  • Track 17-3Ion-mobility Spectrometry
  • Track 17-4Separation Techniques in Analytical Chemistry
  • Track 17-5Analytical Mass Spectrometry of Herbicides
  • Track 17-6Mass Spectrometry in bioinorganic Analytical Chemistry
  • Track 17-7Mass Spectrometry in bioinorganic Analytical Chemistry
  • Track 17-8chromatography
Proteomics is the large-scale study of proteins and proteomes.Proteins are vital parts of  functional living organisms, Proteomics  refers to the large-scale experimental protein purification and mass spectrometry analysis.Proteomic technologies is use for  identification and quantification of overall proteins present content of a cell, tissue or an organism.Mass spectrometry with LC–MS-MS and MALDI-TOF/TOF being widely used equipment is the central among current proteomics.Proteomics is also useful in disease diagnosis,gene function,chromatography ,electrophoresis, Quantitative techniques,crystallography,Bioinformatics analysis..
  • Track 18-1Prteomics application in biomedical
  • Track 18-2Mass Spectrometry involve in Microbial Proteomics
  • Track 18-3Proteomics in Food Science
  • Track 18-4Computational Methods for Mass Spectrometry Proteomics
  • Track 18-5Platelet Proteomics
  • Track 18-6Proteomic Applications in Cancer Detection and Discovery
  • Track 18-7Proteomics in Nephrology