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12th World Congress on Mass Spectrometry, will be organized around the theme “”
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Mass spectrometry – an analytical technique that measures the mass-to-charge ratio of ions and, in forensic science, one of the best ways for toxicologists to identify and analyse substances. As a result, its widest application is in the analysis of drugs (including drug metabolites and drug paraphernalia).
Nuclear magnetic resonance (NMR) spectroscopy is the study of molecules by recording the interaction of radiofrequency (Rf) electromagnetic radiations with the nuclei of molecules placed in a strong magnetic field.
UV spectroscopy or UV–visible spectrophotometry refers to absorption spectroscopy or reflectance spectroscopy in part of the ultraviolet and the full, adjacent visible regions of the electromagnetic spectrum. This means it uses light in the visible and adjacent ranges.
Infrared spectroscopy (IR spectroscopy) is the spectroscopy that deals with the infrared region of the electromagnetic spectrum, that is light with a longer wavelength and lower frequency than visible light. It covers a range of techniques, mostly based on absorption spectroscopy.
Techniques such as ion scattering spectroscopy, which measures the energy reflected from a surface irradiated with an incident ion beam (usually ∼1keV), are not able to discriminate between elements with similar properties, i.e., they cannot distinguish small changes in atomic number or atomic weight.
The use of mass spectrometry in the clinical laboratory has become a standard for analysis of different substances such as antibiotics, for newborn screening, detection of immune-suppressive drugs, or the analysis of therapeutic antibodies used for the treatment of different diseases.
Spectroscopy is the study of the interaction between matter and electromagnetic radiation as a function of the wavelength or frequency of the radiation.
Mass Spectrometry (MS) is a popular technique for environmental analysis because of its ability to carry out sensitive qualitative and quantitative analysis. It lends itself to environmental analysis because it is useful for analyzing analytes in complex mixtures, or with high sample matrix background.
The hyphenated technique is developed from the coupling of a separation technique and an on-line spectroscopic detection technology. Several remarkable improvements in hyphenated analytical methods over the last two decades have significantly broadened their applications in the analysis of biomaterials, especially natural products, pre-isolation analyses of crude extracts or fraction from various natural sources, isolation and detection of natural products, chemical fingerprinting, testing of herbal products, de-replication of natural products, and metabolomics. Rapid identification and characterization of known and new natural products directly from plant and marine sources without the necessity of isolation and purification can be achieved by various modern hyphenated techniques. Techniques like HPLC coupled to NMR (Nuclear Magnetic Resonance) or electrospray ionization tandem mass spectrometry (ESI-MS-MS) have been proven to be extremely powerful tools in natural product analysis, as they aid in the fast screening of crude natural product extracts or fractions for detailed information about metabolic profiles, with minimum quantity of material. Hyphenated HPLC techniques include HPLC-MS, HPLC-ESI-MS, HPLC-IC-MS, HPLC-NMR-MS, HPLC-DAD, HPLC-CE-MS, HPLC-UV, Coupling LC and MALDI-TOF.
- Electrospray Ionization Tandem Mass Spectrometry(ESI-MS-MS)
- Matrix Assisted Laser Desorption Ionization (MALDI)
- Gas Chromatography-Mass Spectrometry(GC-MS)
- Pyrolysis-Gas Chromatography-Mass Spectrometry
Metabolomics and lipidomics aim to profile the wide range of metabolites and lipids that are present in biological samples. Recently, ion mobility spectrometry (IMS) has been used to support metabolomics and lipidomics applications to facilitate the separation and the identification of complex mixtures of analytes.
Proteomics involves the applications of technologies for the 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.current proteomics.
The primary goal of Bio spectroscopy is to form one forum for molecular spectroscopists performing on biological problems and for bio-researchers who wish to use spectroscopy to advance their research. The principal role of Bio spectroscopy is to produce a singular concentrate on the employment of spectroscopy for understanding more about biological molecules.
- Bio Analysis of materials using Spectrometry
High-performance liquid chromatography (HPLC), formerly referred to as high-pressure liquid chromatography, is a technique in analytical chemistry used to separate, identify, and quantify each component in a mixture. It relies on pumps to pass a pressurized liquid solvent containing the sample mixture through a column filled with a solid adsorbent material. Each component in the sample interacts slightly differently with the adsorbent material, causing different flow rates for the different components and leading to the separation of the components as they flow out of the column.
The novelty is to use mass spectrometry to switch radiolabeling and radioactivity measurements, which represent up-to-now the gold standard to live chemical compound concentrations in bioscience. The capacity of ICP-MS to produce high-resolution quantitation of metallic and hetero elements. In contrast to molecular mass spectrometry that produces ions from entire organic entities, elemental mass spectrometry, referred to as inductively coupled plasma-mass spectrometry (ICP-MS), operates at very high temperatures (up to 8000 K) allowing to interrupt all chemical bonds.
- Analysis of metals
- Quality checking of metals
- Analysis of geological materials
Analyticaltoxicology is that the use of the whole range of qualitative and quantitative chemical, immunochemical, and physical techniques utilized in sample preparation, separation, assay calibration, detection and identification, and quantification for the purposes of toxicological research and testing.
Bioanalysis is a term generally used to describe the quantitative measurement of a compound (drug) or their metabolite in biological fluids, primarily blood, plasma, serum, urine or tissue extracts.
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 chromatography. 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. Mass spectrometry is an analytical method 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.
- Mass Spectrometry in the Pharmaceutical Industry
- Chromatography 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 Polymers and Molecular Surfaces/Films
- MS Approaches in Carbohydrates, Microbes and Biomolecule Analysis
- Lipidomics, Metabolomics and Ultratrace Analysis
Looking further into the future, we can expect the trend toward increasing automation ultimately to result in the introduction of fully automated clinical analyzers using mass spectrometry-based detection, at which point mass spectrometry will become widely used by smaller clinical laboratories.
There are many varieties of ionization methods are utilized in mass spectrometry methods. The classic methods that most chemists are accustomed to are electron impact (EI) and Fast Atom Bombardment (FAB). These techniques don't seem to be used much with modern mass spectrometry except EI for environmental work using GC-MS. More modern techniques of and other derivative methods have taken their place within the mass spectrometry laboratory. Ionization mass spectrometry which has become an undeniably essential system inside the clinical lab for assisting examination or quantitative estimation of metabolites during a complex natural sample. MS/MS applications are abundant. Mass spectrometry is an investigative strategy with high explicitness and a developing nearness in research center prescription. various kinds of mass spectrometers are being utilized in enormous number of clinical research facilities over the world, and, thus, noteworthy upgrades in test execution are happening quickly in regions like toxicology, endocrinology, and biochemical markers. This review is a fundamental prologue to mass spectrometry.
- Gas pressure chemical Ionization (APCI)
- Electrospray ionization (ESI)
- Matrix-assisted laser desorption ionization (MALDI)
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.
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.
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.
- Single-cell MALDI Mass Spectrometry Imaging
- Biomolecular Imaging Mass Spectrometry
- Mass Spectrometry Imaging Approaches and Applications
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.
- Proteomics from Discovery to Function and Its Applications
- Analytical Science and Separation Techniques
- Mass Spectrometry Data Analysis in Proteomics
Mass spectrometry (MS) is a powerful analytical tool with many applications in pharmaceutical and biomedical field. 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 spectrometry (MS) is a high-throughput analytical detection technique used to get information about the molecular weights and chemical structures of the peptides, proteins, carbohydrates, oligonucleotides, natural products, and drug metabolites.