OCT 24 - 25 2018

Analytical Chemistry 2018

Our First Annual Analytical Chemistry Virtual Event is now available On Demand!

The field of analytical chemistry is focused on advancements in experimental design, chemometrics, and the creation of new analytical instrumentation. Analytical chemistry has broad applications into forensics, environmental testing, pharmacological developments, material science and engineering.

Join us for this free event as we discuss best practices in testing, chromatography, centrifugation, as well as developments in chemical analysis and mass spectroscopy. Our virtual conference allows you to participate in a global setting with no travel or cost to you. You can participate in exactly those parts which you are interested in and be back at your desk or bench in an instant. Virtual events remove time and place restrictions and ensure that everyone who wants to participate can do so. This virtual conference also offers increased reach for the global analytical chemistry community with a high degree of interaction through live-streaming video and chat sessions.

Topic's for this years event included:

Mass Spectrometry
Imaging Applications
Chemical Sensors & Detectors
FT-IR
Lab-on-a-Chip
Nanofluidics

Call for Speakers —We are always looking to feature excellent research during our virtual events. If you’re working on some remarkable breakthroughs and would like to submit a speaker or panel for consideration, please submit your abstract here.

Continuing Education
By participating in this virtual event and watching webcast presentations, you can earn Free Continuing Education (PACE) credits. To earn educational credits, you must view an entire presentation. Following the presentation, you must click on the educational credit link provided for that particular speaker and follow the required process. Once you have completed the process, you will receive a certificate for the educational credit.

Don't forget to participate in our Leaderboard and Scavenger Hunt to win one of our Free Science T-shirts!

Use #LRanalyticalchem to follow the conversation!

Speakers

Barbara Bojko, PhD

University Professor, Canada Research Chair, Department of Chemistry, University of Waterloo
BIOGRAPHY
Janusz Pawliszyn, PhD

University Professor, Canada Research Chair, Department of Chemistry, University of Waterloo
BIOGRAPHY
Jonathan Sweedler, PhD

Director, School of Chemical Sciences, University of Illinois at Urbana-Champaign
BIOGRAPHY
Luke Arbogast, PhD

Research Chemist, Macromolecular Structure and Function Group, National Institute of Standards and Technology (NIST)
BIOGRAPHY
Giuseppe Bonifazi, PhD

Full Professor, University of Rome "La Sapienza"
BIOGRAPHY
Christopher Chouinard, PhD

Assistant Professor of Chemistry, Department of Biomedical and Chemical Engineering and Sciences (BCES), Florida Institute of Technology
BIOGRAPHY
Jeffrey Hudgens, PhD

Research Chemist, IBBR Fellow, Institute for Bioscience and Biotechnology Research, BioProcess Measurements Group, Biomolecular Measurement Division, National Institute of Standards and Tech
BIOGRAPHY
Richard Larsen, PhD

Senior Product Specialist, Anton Paar USA
BIOGRAPHY
Jessica McVay

Technical Support Specialist, Metrohm
BIOGRAPHY
Kirsty Penkman, PhD

Reader in Analytical Chemistry, Chair of Chemistry Graduate School, Department of Chemistry, University of York
Rena Robinson, PhD

Associate Professor of Chemistry, Vanderbilt University
BIOGRAPHY
Lori Spafford

Product Manager for Titration, Metrohm
BIOGRAPHY

Show Resources

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Posters

Agenda

Download Agenda

OCT 25, 2018 12:00 PM PDT

Through the Looking Glass, and What Amino Acids Found There

Kirsty Penkman, PhD

Reader in Analytical Chemistry, Chair of Chemistry Graduate School, Department of Chemistry, University of York

Analytical chemistry can take you to strange places - for me it has been to the bottom of a quarry, being covered in dirt, excavating sesame-seed sized fossils that allow us to work out when prehistoric creatures such as mammoths and Neanderthals roamed Europe. Being able to identify (and isolate) a fraction of the protein contained within particular fossil shells which degrades at a predictable rate has allowed the development of a robust dating technique. This 'intra-crystalline' protein behaves as a closed system, and if this is targeted in a tiny calcite fossil (snail opercula, the little lids that close the aperture of snail shells) we can date back to at least 2.8 Ma. With LC and MS analyses of protein in fossil material ranging from Great Barrier Reef corals to South African ostrich eggshell and Antarctic ice cores, the chirality of amino acids has helped us unravel the complexities of our past climate as well as providing insights into biomineralisation.

Learning Objectives:

1. How critical it is to understand exactly where your molecules of interest are, and how they can be affected by their environment.
2. The importance of using multiple analytical techniques to provide complementary data.

SEE ABSTRACT HIDE ABSTRACT

Watch Webinar
OCT 25, 2018 10:30 AM PDT

Trash or Treasure: Optimizing Titration Electrodes and Consumables

Jessica McVay, Lori Spafford

Sponsored By: Metrohm USA

Everyone that uses titration in their lab knows how simple and fast the technique can be. However, uncertainty around when to replace electrodes creates confusion. Reagent quality, tubing connections and sample matrix can cause symptoms that mimic an expiring electrode. Understanding these influences and the proper maintenance of your electrode improves lab operations and increases confidence in your results.

Attend this webinar and gain the knowledge to confidently evaluate your system and decide with certainty when to replace the electrode. Hear from Jessica McVay, Technical Support Specialist at Metrohm USA, on her top 5 simple ways to know when to replace your electrode and Lori Spafford, Product Manager at Metrohm USA, on how you can responsibly dispose of your retired electrodes.

Knowing exactly when to replace your electrode ensures accurate results without the fear of wasting valuable lab time and resources.

Learning Objectives:

1. Understand how to troubleshoot a titration system
2. Hear 5 simple ways to identify an electrode that needs replacement
3. Learn how to responsibly dispose of your retired electrodes

SEE ABSTRACT HIDE ABSTRACT

Watch Webinar

Jessica McVay
Technical Support Specialist, Metrohm
BIOGRAPHY

Lori Spafford
Product Manager for Titration, Metrohm
BIOGRAPHY
OCT 25, 2018 9:00 AM PDT

Advances in Hydrogen-Deuterium Exchange Mass Spectrometry That Can Improve Studies of Biosimilars and Membrane Protein Drug Targets

Jeffrey Hudgens, PhD

Research Chemist, IBBR Fellow, Institute for Bioscience and Biotechnology Research, BioProcess Measurements Group, Biomolecular Measurement Division, National Institute of Standards and Tech
BIOGRAPHY

Hydrogen-deuterium exchange mass spectrometry (HDX-MS) has developed into a powerful tool for investigating biopharmaceuticals, protein interactions, and membrane protein dynamics. Since 2010 HDX-MS data has helped substantiate and protect >110 US patents. Increasingly, biopharma companies provide HDX-MS data to support their biologics license applications (BLAs). However, for HDX-MS to emerge as a tool for quality control and similarity evaluations of biotherapeutics, an understanding of HDX-MS reproducibility is needed. NIST has determined the precision of bottom-up HDX-MS (Figure 1) by the analysis of 78,900 peptide measurements from 15 laboratories. We have also developed improvements to HDX-MS methodology, including automated measurements of membrane protein drug targets and chromatography instrumentation, operating at -30 oC, that improves HDX-MS measurements by arresting back-exchange.

Learning Objectives:

1. An interlaboratory comparison involving 15 laboratory cohort has established reproducibility of HDX-MS, facilitating its use in commerce.
2. NIST has developed a method that allows automated HDX-MS studies of membrane proteins, which comprise 60% of all drug targets.
3. Chromatography at -30 oC reduces H for D back-exchange to 5 %, which improves the D-uptake measurement by 3x to 10x.

SEE ABSTRACT HIDE ABSTRACT

Watch Webinar
OCT 25, 2018 7:30 AM PDT

Analytical Approaches to Advance Alzheimer's Disease Research

Rena Robinson, PhD

Associate Professor of Chemistry, Vanderbilt University
BIOGRAPHY

Alzheimer’s disease is becoming a public health crisis as the anticipated number of sufferers is expected to rise to 15 million in the next 30 years, at least in the US. These numbers are exacerbated when considering global incidences of disease. One strategy to combat this rise is to use ‘omics based approaches to better understand the complexity of the disease and to find biomarkers that can be useful for early disease diagnosis. Ultimately, it is desirable for these ‘omics approaches to lead to therapeutic targets and strategies to slow, prevent, or cure disease.

The RASR laboratory develops high-throughput proteomics approaches to understand health disparities in Alzheimer’s disease and the role of the periphery. In this presentation, Dr. Robinson will introduce how her laboratory is approaching these problems through the development of enhanced sample multiplexing techniques. Specifically, an approach developed in her laboratory, combined precursor isotopic labeling and isobaric tagging (cPILOT), has been demonstrated on up to 24 samples that can be analyzed in a single experiment. This capability has allowed studies that evaluate proteomic changes across multiple tissue types, genotypes, and ethnic populations. While there are inherent tradeoffs with a dual labeling approach the benefits gained in cost and time savings and comprehensive quantitative information are extremely valuable for this platform. These tradeoffs will be highlighted as well as considerations for the utility of enhanced multiplexing in enabling studies of Alzheimer’s disease.

Learning Objectives:

1. Participants will learn two approaches for chemically labeling peptides in complex mixtures that can ultimately be combined into a single enhanced multiplexing approach.
2. Participants will become familiar with the benefits and challenges of multiplexed proteomics analyses.
3. Participants will understand how Alzheimer’s disease research can be advanced using multiplexing strategies.

SEE ABSTRACT HIDE ABSTRACT

Watch Webinar
OCT 24, 2018 1:30 PM PDT

Accessories and Techniques for FT-IR Sample Analysis

Richard Larsen, PhD

Senior Product Specialist, Anton Paar USA
BIOGRAPHY

This intensive workshop will introduce infrared spectroscopy, outline the various sample handling methods and provide guidance on the numerous transmission and reflectance methods available for infrared analysis.

Concepts of infrared absorption spectroscopy will be introduced with a discussion of sample analysis methods and the wide selection of accessories used to obtain representative infrared spectra of analytical samples. Methods for obtaining the 'ideal' spectrum will be presented as well as how to get the most out of the large variety of available FT-IR sampling accessories. The common pitfalls to avoid during sample preparation will also be examined. Sampling techniques for transmission measurements using KBr pellets, mulls, liquid cells and films will be outlined in addition to presentations on Multiple Internal Reflectance (MIR, HATR), Diffuse Reflectance (DRIFTS), Specular Reflectance, Reflection-Absorption Spectroscopy (RAIRS) and Grazing Angle measurements. The various transmission and reflectance measurement experiments will be examined to determine which method, or accessory, can provide the infrared data required of specific samples. This workshop is intended for those participants just beginning infrared analysis up to participants interested in more advanced methods of infrared sample analysis.

Learning Objectives:

1. To review the basic theory of infrared absorption spectroscopy.
2. To understand the various methods and accessories available to collect spectra as well as the advantages and disadvantages of the various accessories and methods.

SEE ABSTRACT HIDE ABSTRACT

Watch Webinar
OCT 24, 2018 12:00 PM PDT

Ion Mobility-Mass Spectrometry in the -Omics

Christopher Chouinard, PhD

Assistant Professor of Chemistry, Department of Biomedical and Chemical Engineering and Sciences (BCES), Florida Institute of Technology
BIOGRAPHY

Ion mobility-mass spectrometry (IM-MS) is a rapid, gas-phase separation technique that has become an integral part of the analytical repertoire of techniques for the -omics. This method couples well with existing protocols (i.e., LC-MS) by affording an additional dimension of separation, and provides a characteristic measure of an analyte’s size, shape, and charge in the form of a collision cross section (CCS). CCS can be used to increase confidence in quantitative measurement of known compounds, thus reducing interferences and improving S:N ratios, and also serves as a defining feature in identification of unknowns. Furthermore, this separation based on structure (as opposed to mass-to-charge alone) allows for distinction of structural and stereoisomers of potential biological importance.

This presentation will cover the basic operating principles of IMS and current instrumentation; applications to metabolomics, lipidomics, and proteomics; and future directions for IM-MS, such as implementation in routine clinical analysis.

Learning Objectives:

1. Understand the basic operating principles of IMS and current instrumentation
2. Understand current applications to metabolomics, lipidomics, and proteomics

SEE ABSTRACT HIDE ABSTRACT

Watch Webinar
OCT 24, 2018 10:30 AM PDT

Chemometric Methods for Analysis of 2D 1H-13C Methyl NMR Spectra of Monoclonal Antibodies for Higher Order Structure Characterization

Luke Arbogast, PhD

Research Chemist, Macromolecular Structure and Function Group, National Institute of Standards and Technology (NIST)
BIOGRAPHY

Two-dimensional (2D) 1H-13C methyl correlated NMR is increasingly being recognized as a powerful tool to characterize the higher order structure (HOS) of monoclonal antibody (mAb) therapeutics. 2D methyl NMR is well suited to the task as spectra can be readily be acquired on intact mAbs at natural isotopic abundance, and even small changes to chemical environment and structure manifest observable changes in the spectra, which can be interpreted at atomic resolution. This makes it possible to apply 2D NMR approaches directly to drug products in order to systematically characterize structural effects. Traditionally, such analysis has involved identifying specific changes to measured resonance peak parameters. Recently, we have demonstrated a complementary approach using principal component analysis (PCA) to directly analyze the matrix of spectral data, correlating spectra according to similarities and differences in their overall shapes. This approach is particularly well-suited for spectra of mAbs, where many individual peaks may not be well resolved and peak parameters difficult to measure. Here we demonstrate the performance of the PCA method for discriminating structural variation among systematic sets of 2D NMR spectra using the NISTmAb reference material and illustrate how spectral variability identified by PCA may be correlated to structure.

Learning Objectives:

1. 2D 1H-13C Methyl NMR spectra can be readily acquired on monoclonal antibody therapeutics at natural isotopic abundance.
2. Such spectra are suitable to assess the major conformation(s) of mAb drugs in solution.
3. Using multivariate statistics, such as principal component analysis mAb spectra can be classified based on minor structural perturbations with low levels of detection.

SEE ABSTRACT HIDE ABSTRACT

Watch Webinar
OCT 24, 2018 9:00 AM PDT

Keynote Presentation: Solid Phase Microextraction: New Developments in Bioanalysis and Medical Applications

Barbara Bojko, PhD, Janusz Pawliszyn, PhD

Solid phase microextraction (SPME) is a versatile, non-exhaustive sample preparation tool that has been demonstrated to be well-suited for facile and effective analysis of a broad range of compounds in a plethora of studies. A growing number of reports describing diverse SPME workflows for novel investigations in a variety of fields including diverse bioanalytical applications, among others, corroborate the applicability of this microextraction tool in the bioanalytical sciences. Important bioanalytical applications of SPME include high throughput, in vivo and on-site analysis, in vitro and in vivo metabolomics studies, pharmaceutical and biomedical research. Patient monitoring, metabolomics and biomarkers discovery are an integral part of medical diagnosis and biomedical research. However, tissue analysis remains the bottleneck of such studies due to the invasiveness of presently used sample collection based on biopsy, as well as the laborious and time-consuming sample preparation protocols. In the proposed technology, we have integrated in vivo sampling, sample preparation including global extraction of metabolites together with convenient coupling to analytical instrument. This approach based on a small sorbent coated flexible metal fiber format of solid phase microextraction was developed and evaluated during organ treatment and transplantation in pig model as well as applied to human organs. In this chemical biopsy approach, only molecules of interests are extracted onto biocompatible sorbent from the investigated system, however tissue is not removed from the organ, just metabolites of interest. When using extraction phase with appropriate chemical property and morphology, the analytes are enriched onto the sorbent with minimum of interferences collected. Therefore, the direct coupling of the chemical biopsy probe to mass spectrometry is feasible. Such hyphenation facilitates rapid on-site quantification of the compounds of interests resulting in possibility of close to real time monitoring. This approach has potential in biological and clinical on-site investigations including bedside medical diagnosis.

Learning Objectives:

1. Provide understanding about microextraction approaches and their advantages compared to exhaustive extraction techniques.
2. To demonstrate potential of the SPME technology in biomedical research.

SEE ABSTRACT HIDE ABSTRACT

Watch Webinar

Barbara Bojko, PhD
University Professor, Canada Research Chair, Department of Chemistry, University of Waterloo
BIOGRAPHY

Janusz Pawliszyn, PhD
University Professor, Canada Research Chair, Department of Chemistry, University of Waterloo
BIOGRAPHY
OCT 24, 2018 7:30 AM PDT

Keynote Presentation: Mass Spectrometry Approaches for the the Single Cell Chemical Characterization of the Brain

Jonathan Sweedler, PhD

Director, School of Chemical Sciences, University of Illinois at Urbana-Champaign
BIOGRAPHY

In the postgenomic era, one expects the suite of chemical players in a brain region to be known and their functions uncovered. Perhaps surprisingly, many neurochemicals remain poorly characterized and for those that are known, their localization, dynamics and function are oftentimes unknown. Several approaches for assaying the chemical content within targeted brain regions and from individual brain cells are highlighted, including mass spectrometry imaging (MSI) and MS-based single cell measurements. Using these approaches, we can measure lipids, fatty acids, neurotransmitters and neuropeptides, among others. For single cell measurements, the cells of interest are scattered across a microscope slide, the exact cell positions determined via optical microscopy, and mass spectra are acquired only at the cell positions. The single cell assays allow differences in the metabolome and peptidome from supposedly homogeneous populations of cells to be explored. By obtaining information from tens of thousands of individual cells, rare cells are found and unusual neurochemicals are discovered. For select cells, follow-up capillary electrophoresis-mass spectrometry and other information rich assays can be performed. Several applications of single cell mass spectrometry are highlighted from the discovery of unusual metabolites to characterizing the both known and previously unknown neuropeptides and hormones in single cells. Our overarching goal is to uncover the complex chemical mosaic of the brain and pinpoint key cellular players involved in a range of physiological and pathological processes.

Learning Objectives:

1. Participants will understand why single cell measurements important.
2. Participants will describe the importance and how cells are prepared and measured with mass spectrometry.
3. Participants will learn about the chemical information gained from single cell mass spectrometry measurements and how it relates to cell function, health and disease.

SEE ABSTRACT HIDE ABSTRACT

Watch Webinar
OCT 24, 2018 6:00 AM PDT

Applied Hyperspectral Imaging Fundamentals and Case Studies

Giuseppe Bonifazi, PhD

Full Professor, University of Rome "La Sapienza"
BIOGRAPHY

A fast, reliable and low cost characterization of materials/ products as fed to a process, and/or resulting from different processing actions, represents one of the most challenging targets in the industry, with reference to several sectors (i.e. primary and secondary raw materials, environment, food industry, pharmaceutical, etc.). Today, thanks to the strong technological development, different techniques are available according to different sampling strategies and analytical principles to detect specific physical-chemical attributes of materials/products, representing the key factor to perform a full process monitoring and/or to apply specific control/tuning actions on the process itself. The attributes can be determined off-line (e.g. sample collection and laboratory scale analyses) or on-line (e.g. direct collection from the products flow stream of the information of interest). In this Webminar (ID#: 1216951) the principles and the possibilities offered by the adoption of specialized devices allowing to develop on-line acquisition/processing strategies, based on HyperSpectral Imaging (HSI) and finalised to perform materials/products streams characterization, inspection and quality control actions, are presented and discussed.

Learning Objectives:

1. HyperSpectral Imaging (HSI) based techniques fundamentals.
2. Analytical applicative potentialities of HyperSpectral Imaging (HSI) with reference to both “off-line” and “on-line” applications addressed to qualitatively and quantitatively assess materials and/or products characteristics.

SEE ABSTRACT HIDE ABSTRACT

Watch Webinar

Imaging Applications
OCT 24, 2018 6:00 AM PDT

Applied Hyperspectral Imaging Fundamentals and Case Studies

Giuseppe Bonifazi, PhD

Full Professor, University of Rome "La Sapienza"
BIOGRAPHY

A fast, reliable and low cost characterization of materials/ products as fed to a process, and/or resulting from different processing actions, represents one of the most challenging targets in the industry, with reference to several sectors (i.e. primary and secondary raw materials, environment, food industry, pharmaceutical, etc.). Today, thanks to the strong technological development, different techniques are available according to different sampling strategies and analytical principles to detect specific physical-chemical attributes of materials/products, representing the key factor to perform a full process monitoring and/or to apply specific control/tuning actions on the process itself. The attributes can be determined off-line (e.g. sample collection and laboratory scale analyses) or on-line (e.g. direct collection from the products flow stream of the information of interest). In this Webminar (ID#: 1216951) the principles and the possibilities offered by the adoption of specialized devices allowing to develop on-line acquisition/processing strategies, based on HyperSpectral Imaging (HSI) and finalised to perform materials/products streams characterization, inspection and quality control actions, are presented and discussed.

Learning Objectives:

1. HyperSpectral Imaging (HSI) based techniques fundamentals.
2. Analytical applicative potentialities of HyperSpectral Imaging (HSI) with reference to both “off-line” and “on-line” applications addressed to qualitatively and quantitatively assess materials and/or products characteristics.

SEE ABSTRACT HIDE ABSTRACT

Watch Webinar
OCT 24, 2018 9:00 AM PDT

Keynote Presentation: Solid Phase Microextraction: New Developments in Bioanalysis and Medical Applications

Barbara Bojko, PhD, Janusz Pawliszyn, PhD

Solid phase microextraction (SPME) is a versatile, non-exhaustive sample preparation tool that has been demonstrated to be well-suited for facile and effective analysis of a broad range of compounds in a plethora of studies. A growing number of reports describing diverse SPME workflows for novel investigations in a variety of fields including diverse bioanalytical applications, among others, corroborate the applicability of this microextraction tool in the bioanalytical sciences. Important bioanalytical applications of SPME include high throughput, in vivo and on-site analysis, in vitro and in vivo metabolomics studies, pharmaceutical and biomedical research. Patient monitoring, metabolomics and biomarkers discovery are an integral part of medical diagnosis and biomedical research. However, tissue analysis remains the bottleneck of such studies due to the invasiveness of presently used sample collection based on biopsy, as well as the laborious and time-consuming sample preparation protocols. In the proposed technology, we have integrated in vivo sampling, sample preparation including global extraction of metabolites together with convenient coupling to analytical instrument. This approach based on a small sorbent coated flexible metal fiber format of solid phase microextraction was developed and evaluated during organ treatment and transplantation in pig model as well as applied to human organs. In this chemical biopsy approach, only molecules of interests are extracted onto biocompatible sorbent from the investigated system, however tissue is not removed from the organ, just metabolites of interest. When using extraction phase with appropriate chemical property and morphology, the analytes are enriched onto the sorbent with minimum of interferences collected. Therefore, the direct coupling of the chemical biopsy probe to mass spectrometry is feasible. Such hyphenation facilitates rapid on-site quantification of the compounds of interests resulting in possibility of close to real time monitoring. This approach has potential in biological and clinical on-site investigations including bedside medical diagnosis.

Learning Objectives:

1. Provide understanding about microextraction approaches and their advantages compared to exhaustive extraction techniques.
2. To demonstrate potential of the SPME technology in biomedical research.

SEE ABSTRACT HIDE ABSTRACT

Watch Webinar

Barbara Bojko, PhD
University Professor, Canada Research Chair, Department of Chemistry, University of Waterloo
BIOGRAPHY

Janusz Pawliszyn, PhD
University Professor, Canada Research Chair, Department of Chemistry, University of Waterloo
BIOGRAPHY
Mass Spectrometry
OCT 24, 2018 7:30 AM PDT

Keynote Presentation: Mass Spectrometry Approaches for the the Single Cell Chemical Characterization of the Brain

Jonathan Sweedler, PhD

Director, School of Chemical Sciences, University of Illinois at Urbana-Champaign
BIOGRAPHY

In the postgenomic era, one expects the suite of chemical players in a brain region to be known and their functions uncovered. Perhaps surprisingly, many neurochemicals remain poorly characterized and for those that are known, their localization, dynamics and function are oftentimes unknown. Several approaches for assaying the chemical content within targeted brain regions and from individual brain cells are highlighted, including mass spectrometry imaging (MSI) and MS-based single cell measurements. Using these approaches, we can measure lipids, fatty acids, neurotransmitters and neuropeptides, among others. For single cell measurements, the cells of interest are scattered across a microscope slide, the exact cell positions determined via optical microscopy, and mass spectra are acquired only at the cell positions. The single cell assays allow differences in the metabolome and peptidome from supposedly homogeneous populations of cells to be explored. By obtaining information from tens of thousands of individual cells, rare cells are found and unusual neurochemicals are discovered. For select cells, follow-up capillary electrophoresis-mass spectrometry and other information rich assays can be performed. Several applications of single cell mass spectrometry are highlighted from the discovery of unusual metabolites to characterizing the both known and previously unknown neuropeptides and hormones in single cells. Our overarching goal is to uncover the complex chemical mosaic of the brain and pinpoint key cellular players involved in a range of physiological and pathological processes.

Learning Objectives:

1. Participants will understand why single cell measurements important.
2. Participants will describe the importance and how cells are prepared and measured with mass spectrometry.
3. Participants will learn about the chemical information gained from single cell mass spectrometry measurements and how it relates to cell function, health and disease.

SEE ABSTRACT HIDE ABSTRACT

Watch Webinar
OCT 24, 2018 12:00 PM PDT

Ion Mobility-Mass Spectrometry in the -Omics

Christopher Chouinard, PhD

Assistant Professor of Chemistry, Department of Biomedical and Chemical Engineering and Sciences (BCES), Florida Institute of Technology
BIOGRAPHY

Ion mobility-mass spectrometry (IM-MS) is a rapid, gas-phase separation technique that has become an integral part of the analytical repertoire of techniques for the -omics. This method couples well with existing protocols (i.e., LC-MS) by affording an additional dimension of separation, and provides a characteristic measure of an analyte’s size, shape, and charge in the form of a collision cross section (CCS). CCS can be used to increase confidence in quantitative measurement of known compounds, thus reducing interferences and improving S:N ratios, and also serves as a defining feature in identification of unknowns. Furthermore, this separation based on structure (as opposed to mass-to-charge alone) allows for distinction of structural and stereoisomers of potential biological importance.

This presentation will cover the basic operating principles of IMS and current instrumentation; applications to metabolomics, lipidomics, and proteomics; and future directions for IM-MS, such as implementation in routine clinical analysis.

Learning Objectives:

1. Understand the basic operating principles of IMS and current instrumentation
2. Understand current applications to metabolomics, lipidomics, and proteomics

SEE ABSTRACT HIDE ABSTRACT

Watch Webinar
OCT 25, 2018 9:00 AM PDT

Advances in Hydrogen-Deuterium Exchange Mass Spectrometry That Can Improve Studies of Biosimilars and Membrane Protein Drug Targets

Jeffrey Hudgens, PhD

Research Chemist, IBBR Fellow, Institute for Bioscience and Biotechnology Research, BioProcess Measurements Group, Biomolecular Measurement Division, National Institute of Standards and Tech
BIOGRAPHY

Hydrogen-deuterium exchange mass spectrometry (HDX-MS) has developed into a powerful tool for investigating biopharmaceuticals, protein interactions, and membrane protein dynamics. Since 2010 HDX-MS data has helped substantiate and protect >110 US patents. Increasingly, biopharma companies provide HDX-MS data to support their biologics license applications (BLAs). However, for HDX-MS to emerge as a tool for quality control and similarity evaluations of biotherapeutics, an understanding of HDX-MS reproducibility is needed. NIST has determined the precision of bottom-up HDX-MS (Figure 1) by the analysis of 78,900 peptide measurements from 15 laboratories. We have also developed improvements to HDX-MS methodology, including automated measurements of membrane protein drug targets and chromatography instrumentation, operating at -30 oC, that improves HDX-MS measurements by arresting back-exchange.

Learning Objectives:

1. An interlaboratory comparison involving 15 laboratory cohort has established reproducibility of HDX-MS, facilitating its use in commerce.
2. NIST has developed a method that allows automated HDX-MS studies of membrane proteins, which comprise 60% of all drug targets.
3. Chromatography at -30 oC reduces H for D back-exchange to 5 %, which improves the D-uptake measurement by 3x to 10x.

SEE ABSTRACT HIDE ABSTRACT

Watch Webinar
Chemical Sensors & Detectors
OCT 24, 2018 10:30 AM PDT

Chemometric Methods for Analysis of 2D 1H-13C Methyl NMR Spectra of Monoclonal Antibodies for Higher Order Structure Characterization

Luke Arbogast, PhD

Research Chemist, Macromolecular Structure and Function Group, National Institute of Standards and Technology (NIST)
BIOGRAPHY

Two-dimensional (2D) 1H-13C methyl correlated NMR is increasingly being recognized as a powerful tool to characterize the higher order structure (HOS) of monoclonal antibody (mAb) therapeutics. 2D methyl NMR is well suited to the task as spectra can be readily be acquired on intact mAbs at natural isotopic abundance, and even small changes to chemical environment and structure manifest observable changes in the spectra, which can be interpreted at atomic resolution. This makes it possible to apply 2D NMR approaches directly to drug products in order to systematically characterize structural effects. Traditionally, such analysis has involved identifying specific changes to measured resonance peak parameters. Recently, we have demonstrated a complementary approach using principal component analysis (PCA) to directly analyze the matrix of spectral data, correlating spectra according to similarities and differences in their overall shapes. This approach is particularly well-suited for spectra of mAbs, where many individual peaks may not be well resolved and peak parameters difficult to measure. Here we demonstrate the performance of the PCA method for discriminating structural variation among systematic sets of 2D NMR spectra using the NISTmAb reference material and illustrate how spectral variability identified by PCA may be correlated to structure.

Learning Objectives:

1. 2D 1H-13C Methyl NMR spectra can be readily acquired on monoclonal antibody therapeutics at natural isotopic abundance.
2. Such spectra are suitable to assess the major conformation(s) of mAb drugs in solution.
3. Using multivariate statistics, such as principal component analysis mAb spectra can be classified based on minor structural perturbations with low levels of detection.

SEE ABSTRACT HIDE ABSTRACT

Watch Webinar
OCT 25, 2018 10:30 AM PDT

Trash or Treasure: Optimizing Titration Electrodes and Consumables

Jessica McVay, Lori Spafford

Sponsored By: Metrohm USA

Everyone that uses titration in their lab knows how simple and fast the technique can be. However, uncertainty around when to replace electrodes creates confusion. Reagent quality, tubing connections and sample matrix can cause symptoms that mimic an expiring electrode. Understanding these influences and the proper maintenance of your electrode improves lab operations and increases confidence in your results.

Attend this webinar and gain the knowledge to confidently evaluate your system and decide with certainty when to replace the electrode. Hear from Jessica McVay, Technical Support Specialist at Metrohm USA, on her top 5 simple ways to know when to replace your electrode and Lori Spafford, Product Manager at Metrohm USA, on how you can responsibly dispose of your retired electrodes.

Knowing exactly when to replace your electrode ensures accurate results without the fear of wasting valuable lab time and resources.

Learning Objectives:

1. Understand how to troubleshoot a titration system
2. Hear 5 simple ways to identify an electrode that needs replacement
3. Learn how to responsibly dispose of your retired electrodes

SEE ABSTRACT HIDE ABSTRACT

Watch Webinar

Jessica McVay
Technical Support Specialist, Metrohm
BIOGRAPHY

Lori Spafford
Product Manager for Titration, Metrohm
BIOGRAPHY
OCT 25, 2018 12:00 PM PDT

Through the Looking Glass, and What Amino Acids Found There

Kirsty Penkman, PhD

Reader in Analytical Chemistry, Chair of Chemistry Graduate School, Department of Chemistry, University of York

Analytical chemistry can take you to strange places - for me it has been to the bottom of a quarry, being covered in dirt, excavating sesame-seed sized fossils that allow us to work out when prehistoric creatures such as mammoths and Neanderthals roamed Europe. Being able to identify (and isolate) a fraction of the protein contained within particular fossil shells which degrades at a predictable rate has allowed the development of a robust dating technique. This 'intra-crystalline' protein behaves as a closed system, and if this is targeted in a tiny calcite fossil (snail opercula, the little lids that close the aperture of snail shells) we can date back to at least 2.8 Ma. With LC and MS analyses of protein in fossil material ranging from Great Barrier Reef corals to South African ostrich eggshell and Antarctic ice cores, the chirality of amino acids has helped us unravel the complexities of our past climate as well as providing insights into biomineralisation.

Learning Objectives:

1. How critical it is to understand exactly where your molecules of interest are, and how they can be affected by their environment.
2. The importance of using multiple analytical techniques to provide complementary data.

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FT-IR
OCT 24, 2018 1:30 PM PDT

Accessories and Techniques for FT-IR Sample Analysis

Richard Larsen, PhD

Senior Product Specialist, Anton Paar USA
BIOGRAPHY

This intensive workshop will introduce infrared spectroscopy, outline the various sample handling methods and provide guidance on the numerous transmission and reflectance methods available for infrared analysis.

Concepts of infrared absorption spectroscopy will be introduced with a discussion of sample analysis methods and the wide selection of accessories used to obtain representative infrared spectra of analytical samples. Methods for obtaining the 'ideal' spectrum will be presented as well as how to get the most out of the large variety of available FT-IR sampling accessories. The common pitfalls to avoid during sample preparation will also be examined. Sampling techniques for transmission measurements using KBr pellets, mulls, liquid cells and films will be outlined in addition to presentations on Multiple Internal Reflectance (MIR, HATR), Diffuse Reflectance (DRIFTS), Specular Reflectance, Reflection-Absorption Spectroscopy (RAIRS) and Grazing Angle measurements. The various transmission and reflectance measurement experiments will be examined to determine which method, or accessory, can provide the infrared data required of specific samples. This workshop is intended for those participants just beginning infrared analysis up to participants interested in more advanced methods of infrared sample analysis.

Learning Objectives:

1. To review the basic theory of infrared absorption spectroscopy.
2. To understand the various methods and accessories available to collect spectra as well as the advantages and disadvantages of the various accessories and methods.

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Biomarkers
OCT 25, 2018 7:30 AM PDT

Analytical Approaches to Advance Alzheimer's Disease Research

Rena Robinson, PhD

Associate Professor of Chemistry, Vanderbilt University
BIOGRAPHY

Alzheimer’s disease is becoming a public health crisis as the anticipated number of sufferers is expected to rise to 15 million in the next 30 years, at least in the US. These numbers are exacerbated when considering global incidences of disease. One strategy to combat this rise is to use ‘omics based approaches to better understand the complexity of the disease and to find biomarkers that can be useful for early disease diagnosis. Ultimately, it is desirable for these ‘omics approaches to lead to therapeutic targets and strategies to slow, prevent, or cure disease.

The RASR laboratory develops high-throughput proteomics approaches to understand health disparities in Alzheimer’s disease and the role of the periphery. In this presentation, Dr. Robinson will introduce how her laboratory is approaching these problems through the development of enhanced sample multiplexing techniques. Specifically, an approach developed in her laboratory, combined precursor isotopic labeling and isobaric tagging (cPILOT), has been demonstrated on up to 24 samples that can be analyzed in a single experiment. This capability has allowed studies that evaluate proteomic changes across multiple tissue types, genotypes, and ethnic populations. While there are inherent tradeoffs with a dual labeling approach the benefits gained in cost and time savings and comprehensive quantitative information are extremely valuable for this platform. These tradeoffs will be highlighted as well as considerations for the utility of enhanced multiplexing in enabling studies of Alzheimer’s disease.

Learning Objectives:

1. Participants will learn two approaches for chemically labeling peptides in complex mixtures that can ultimately be combined into a single enhanced multiplexing approach.
2. Participants will become familiar with the benefits and challenges of multiplexed proteomics analyses.
3. Participants will understand how Alzheimer’s disease research can be advanced using multiplexing strategies.

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Speakers

CALL FOR SPEAKERS

We are always looking to feature excellent research during our virtual events. If you’re working on some remarkable breakthroughs and would like to submit a speaker or panel for consideration, please submit your abstract here.

Barbara Bojko, PhD

University Professor, Canada Research Chair, Department of Chemistry, University of Waterloo

BIOGRAPHY
Janusz Pawliszyn, PhD

University Professor, Canada Research Chair, Department of Chemistry, University of Waterloo

BIOGRAPHY
Jonathan Sweedler, PhD

Director, School of Chemical Sciences, University of Illinois at Urbana-Champaign

BIOGRAPHY
Luke Arbogast, PhD

Research Chemist, Macromolecular Structure and Function Group, National Institute of Standards and Technology (NIST)

BIOGRAPHY
Giuseppe Bonifazi, PhD

Full Professor, University of Rome "La Sapienza"

BIOGRAPHY
Christopher Chouinard, PhD

Assistant Professor of Chemistry, Department of Biomedical and Chemical Engineering and Sciences (BCES), Florida Institute of Technology

BIOGRAPHY
Jeffrey Hudgens, PhD

Research Chemist, IBBR Fellow, Institute for Bioscience and Biotechnology Research, BioProcess Measurements Group, Biomolecular Measurement Division, National Institute of Standards and Tech

BIOGRAPHY
Richard Larsen, PhD

Senior Product Specialist, Anton Paar USA

BIOGRAPHY
Jessica McVay

Technical Support Specialist, Metrohm

BIOGRAPHY
Kirsty Penkman, PhD

Reader in Analytical Chemistry, Chair of Chemistry Graduate School, Department of Chemistry, University of York
Rena Robinson, PhD

Associate Professor of Chemistry, Vanderbilt University

BIOGRAPHY
Lori Spafford

Product Manager for Titration, Metrohm

BIOGRAPHY

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Analytical Chemistry 2018

Barbara Bojko, PhD

Janusz Pawliszyn, PhD

Jonathan Sweedler, PhD

Luke Arbogast, PhD

Giuseppe Bonifazi, PhD

Christopher Chouinard, PhD

Jeffrey Hudgens, PhD

Richard Larsen, PhD

Jessica McVay

Kirsty Penkman, PhD

Rena Robinson, PhD

Lori Spafford