Please register for each webinar that you plan to attend.

Presenters* include:

Thomas Horvath, PhD | Assistant Professor
Department of Pathology & Immunology
Baylor College of Medicine (USA)
Quantitative Analysis of Bile Acids Using High-Resolution Mass Spectrometry (HRMS)-based Methods

Glenda Courtney-Martin, PhD | Senior Associate Scientist & Assistant Professor
Hospital for Sick Children (SickKids) (Canada)
From Amino Acid and Protein Requirements to Protein Quality: Knowledge Gained from Applying the Stable Isotope-based Indicator Amino Acid Oxidation (IAAO) Method

Nicolaas Deutz, MD, PhD | Professor & Director
The Center for Translational Research in Aging & Longevity
Texas A&M University (USA)
Stable Isotope Pulse Tracer Method in Human Clinical Research

Stacy Dee, PhD | Research & Development Scientist
Labcorp (USA)
Precision with Purr-pose: Overcoming the Challenges of PCATs Assay Development and Validation

Tom Casimir Bamberger, PhD | Research Scientist
Department of Molecular & Structural Biology
The Scripps Research Institute (USA)
Accurate Quantification of Protein Conformations with the Isotope Label-based Bottom-up Proteomics Approach 'Covalent Protein Painting'

Facilitator:

Andrew Percy, PhD
Senior Applications Chemist, Mass Spectrometry
and MS Omics Product Manager
Cambridge Isotope Laboratories, Inc. (USA)

*Presenter biographies and presentation abstracts can be found below.

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Presenters* include:

Haribabu Arthanari, PhD | Associate Professor
Dpartment of Biological Chemistry & Molecular Pharmacology
Harvard Medical School and Dana-Farber Cancer Institute (USA)
TBA

Jeanine Prompers, PhD | Professor
Department of Human Biology
NUTRIM Institute of Nutrition and Translational Research in Metabolism
Maastricht University Medical Centre (Netherlands)
Advances in Deuterium Metabolic Imaging: Paving the Way to Clinical Translation

Yves Aubin, PhD | Research Scientist
Regulatory Research Division, Biologics
and Radiopharmaceutical Drug Directorate
Health Canada (Canada)
Protocol for the Preparation of Fab and Fc Fragments from Therapeutic Monoclonal Antibodies Using Escherichia coli to Speed up Complete Backbone and Near-complete Side-chain Methyl Assignment

Yaqiang Wang, PhD | Assistant Professor
Department of Biophysics
Medical College of Wisconsin (USA)
Isotopic Labeling Strategies for RNA-Targeted Drug Discovery

Facilitator:

Kelly Andrade
Assistant Product Manager – BioNMR, NMR Solvents
Cambridge Isotope Laboratories, Inc. (USA)

*Presenter biographies and presentation abstracts can be found below.

Can’t make it on the specified date and time?
No worries! Register anyway, and we’ll send you a copy of the webinar
(approved recordings only) so you can watch it when convenient.

If you do not receive the confirmation email with login information
within 10 minutes of hitting the submit button please check your spam/junk folder.

Presenters* include:

Rebecca Weed, PhD | Research Scholar
North Carolina State University (USA)
Dirty Water, Clean Data: How We Measure and Detect PFAS Using Stable Isotope Standards

Adrian Covaci, PhD | Professor
Department of Pharmaceutical Sciences
University of Antwerp (Belgium)
Ion Mobility Spectrometry of Quaternary Ammonium Disinfectants

Shoji Nakayama, MD, PhD | Deputy Director
Japan Environment and Children’s Study Programme Office (Japan)
Children’s Environmental Epidemiology and Human Biomonitoring in Japan

Facilitator:

Ben Priest
Business Deveopment Manager – Environmental Products
Cambridge Isotope Laboratories, Inc. (USA)

*Presenter biographies and presentation abstracts can be found below.

Can’t make it on the specified date and time?
No worries! Register anyway, and we’ll send you a copy of the webinar
(approved recordings only) so you can watch it when convenient.

If you do not receive the confirmation email with login information
within 10 minutes of hitting the submit button please check your spam/junk folder.

 Biographies and Abstracts – Mass Spectrometry

Thomas Horvath, PhD | Assistant Professor
Department of Pathology & Immunology
Baylor College of Medicine (USA)

Thomas Horvath, PhD • Assistant Professor, Pathology & Immunology, Baylor College of Medicine • Chief Bioanalytical Chemist, The Virginia & L.E. Simmons Family Foundation Mass Spectrometry Laboratory, Texas Children’s Research Institute – Microbiome Center, Texas Children’s Hospital • Adjunct Professor, Pharmacy Practice & Translational Research, University of Houston • Associate Academic Editor, Cell Press – STAR Protocols. I am an assistant professor in possession of more than 22 years of academic and FDA/EMA-regulated pharmaceutical-industry research experience in the field of bioanalytical chemistry. Over the course of my career, I have developed considerable skill in the development and validation of high-throughput LC-MS/MS-based bioanalytical methods to measure exogenous small-molecule therapeutics (e.g., pharmaceuticals and peptides) or endogenous bio-molecules (e.g., metabolites and lipids) in an assortment of biological matrices and homogenized tissues. I have developed methods to support a host of projects that include: i) PK/PD assessments of therapeutic compounds or therapeutic enzymes; ii) assess the effectiveness or bioequivalence of novel, off-patent formulations; iii) investigate the mechanism of action of new therapeutic compounds; and iv) determine alterations in metabolic pathways based on disease state or therapeutic intervention. My publication record spans a diverse subset of life science research that includes nutritional biochemistry, pharmacokinetics/pharmacodynamics of new pharmaceutical entities, and more recently, analytical microbiology applications including methods to interrogate the mammalian gut-brain-axis.

Quantitative Analysis of Bile Acids Using High-Resolution Mass Spectrometry (HRMS)-based Methods

As interest in bile acid biochemistry and metabolism continues to accelerate in biomedical and life science research, bioanalytical chemists will be charged with the development of more complex methods to perform quantitative analysis on this functionally interesting and ever-expanding class of molecules. The work described in this presentation will focus primarily on several key operational aspects of our newly developed ZenoTOF 7600+-based bioanalytical method and feature some quantitative bile acid data acquired from blood and/or stool specimen extracts. By leveraging the MRMHR scanning capabilities of the ZenoTOF 7600+, we can specify narrow mass-to-charge (m/z) isolation windows in the SCIEX OS Analytics Module to select specific fragment ions or precursor ions in instances where diagnostic fragment ions aren’t produced from full-scan product ion spectra. These narrow m/z isolation windows result in a boost in detection sensitivity (i.e., signal-to-noise) that is comparable to the sensitivity offered by the QTRAP 7500 in my lab for bile acid detection. Together, these data demonstrate the capability of the ZenoTOF 7600+ system to perform highly sensitive and selective analysis of endogenous bile acid content in biological specimen extracts for matrices such as blood plasma or stool.

During this talk you will learn about:

• HRMS-based Instrumentation can be used for quantitative analysis
• Bile acids are an important class of metabolites to study in a number of diseases
• CIL-based bile acid mixtures are critical for my bile acid research program, and we are making big discoveries because of the convenience and ease of use of this product

Glenda Courtney-Martin, PhD | Senior Associate Scientist & Assistant Professor
Hospital for Sick Children (SickKids) (Canada)

Glenda Courtney-Martin is a health clinician scientist and senior associate scientist in the Research Institute, Hospital for Sick Children (SickKids), Toronto, and assistant professor in the Department of Nutritional Sciences and Faculty of Kinesiology at University of Toronto. Her research is focused on protein and amino acid requirements and metabolism across the life cycle and on protein quality of foods for human nutrition. Her current focus is on amino acid requirements in total parenteral nutrition (TPN) fed neonates and in older adults. Her lab is also currently evaluating protein quality of cereal grains and pulse using the indicator amino acid method.

From Amino Acid and Protein Requirements to Protein Quality: Knowledge Gained from Applying the Stable Isotope-based Indicator Amino Acid Oxidation (IAAO) Method

Protein is an indispensable nutrient due to its content of amino acids which must be dietarily derived. Current amino acid requirements for young and older adults are based on data from studies in young adults using the stable isotope based indicator amino acid oxidation (IAAO) method. However, protein recommendations are based on nitrogen balance data. The Institute of Medicine recommends that nitrogen balance no longer be regarded as the gold standard for estimating protein requirements and that new methods be sought. We applied the stable isotope-based IAAO method to study protein requirements in young and older adults and found them to be higher than current recommendations but not different from each other. However, using the IAAO method we demonstrated that requirements for key indispensable amino acid are higher in older adults. This suggest that protein quality is more important for older than for younger adults. With recent plant-based protein recommendations, the study of protein quality is necessary to determine to capacity of plant proteins to meet amino acid needs. The IAAO method was validated to study protein quality of foods and has been applied in humans to assess metabolic availability of limiting amino acids and to test the effect of protein complementation. The objectives of the talk are:

1. To preset the concepts and application of the IAAO method to study amino acid requirements across the lifespan and in vulnerable populations;

2. To present data on the application of the IAAO method to study protein requirements and physiological studies validating the IAAO derived estimates of protein requirements in adults;

3. To present data on the application of the IAAO method to study protein quality of plant protein foods and to assess the effect of complementary protein sources.

During this talk you will learn about:

• Current requirements recommendations for amino acids are based on studies using the stable isotope-based IAAO method.
• Data using the IAAO and stable isotope-based precursor product methodology demonstrate a higher requirement for protein than current recommendations.
• With current national and international recommendations to increase plant protein consumption for health and environmental sustainability, the IAAO method has been successfully applied to study protein quality of foods for human nutrition.

Nicolaas Deutz, MD, PhD | Professor & Director
The Center for Translational Research in Aging and Longevity
Texas A&M University (USA)

Dr. Deutz is a professor and the director for the Center for Translational Research in Aging & Longevity at Texas A&M University. His research interests are in clinical nutrition and metabolism in animals and humans for more than 40 years and he has published over 400 papers. His clinical interest is using nutritional supplements to treat malnutrition in older adults and during acute and chronic disease states. His research focuses on (inter)organ protein and amino acid metabolism using animals (mice, rats, pigs), healthy humans, and patients with various acute and chronic diseases, including sepsis, (pre)diabetes, obesity, cancer, and COPD. As PI, he has conducted many federal and industry-sponsored research projects. Since 1988, he has been an active member of the European Society of Clinical Nutrition and Metabolism (ESPEN) and chaired the scientific committee from 2000 - 2005. Since 2006 to 2025, he has been the editor-in-chief of the society's journals.

Stable Isotope Pulse Tracer Method in Human Clinical Research

Stable isotope infusions in humans have been used for many decades to estimate the production of amino acids and to calculate net protein breakdown. The primed-constant and continuous infusion protocol was most often used and measurements were done in the tracer steady state condition, both in the postabsorptive as well as during and after a meal. The main disadvantages of using this approach are the need for steady state conditions with sometimes long infusion times, the need for large amounts of isotopes and the fact that the appearance of the amino acids was measured in plasma as a proxy for the appearance intracellularly. We used the pulse tracer approach to circumvent these disadvantages and also to enable compartmental analysis to measure the intracellular production. We developed a protocol in which we give a mixture of 27 different isotopes of amino acids and related products to estimate the production and size of the extracellular and intracellular pools. We applied the model in a variety of different conditions like COPD, older age, ICU. We recently recalculated the net protein breakdown in humans and established different rates than was estimated in the past. We also applied the pulse isotope approach during feeding.

During this talk you will learn about:

• Difference between primed constant infusion and pulse infusion of stable isotopes
• Pulse tracer approaches and compartmental analysis gives information about intracellular metabolism
• Pulse tracer studies can be done in large groups and humans to increase our understanding of metabolism changes during disease

Stacy Dee, PhD | Research & Development Scientist
Labcorp (USA)

I am a research and development scientist at Labcorp with over 18 years of laboratory experience, including 12 years in R&D. My current work focuses on the development and validation of high-throughput LC-MS/MS assays for small molecules. I have experience in a range of extraction techniques, including liquid-liquid extraction (LLE), solid-phase extraction (SPE), protein precipitation (PPT), and isotope dilution. I have presented some of my research at the American Society for Mass Spectrometry (ASMS) Conferences in 2013, 2014, 2019, 2023, and 2025.

Precision with Purr-pose: Overcoming the Challenges of PCATs Assay Development and Validation

Plasma catecholamine (dopamine, epinephrine, and norepinephrine) measurement helps physicians diagnose the presence of catecholamine-secreting tumors such as pheochromocytomas and paragangliomas when plasma metanephrines testing is inconclusive. Developing a clinical assay for plasma catecholamines (PCATs) requires measuring low concentrations. This presents several challenges. First, PCAT levels in a patient can be affected by medication, food, and even physical activity, therefore patient preparation is crucial. Next, catecholamines are grossly unstable so samples must be handled carefully during collection, shipment, and extraction. Further, separation and quantification are complicated by analyte polarity and the potential presence of interfering medications and metabolites. This presentation will highlight solutions to these challenges in the development and rigorous validation of our high-throughput PCATs assay.

During this talk you will learn about:

• Challenges of measuring low levels of unstable analytes in plasma
• The advantage of using ¹³C-labeled internal standards
• Exemplar validation of a lab-developed test for clinical diagnostics

Tom Casimir Bamberger, PhD | Research Scientist
Department of Molecular & Structural Biology
The Scripps Research Institute (USA)

Tom Casimir Bamberger, PhD, is a research scientist in the Department of Integrative Structural and Computational Biology at The Scripps Research Institute in La Jolla, California. His research centers on the development and application of advanced protein footprinting technologies to detect changes in protein conformation and protein-protein interactions using mass spectrometry-based bottom-up proteomics. His work focuses on aberrant protein folding events that are associated with human diseases, with an emphasis on neurodegenerative disorders. Dr. Bamberger leads the development of Covalent Protein Painting, a technology platform that enables the discovery of novel disease-related protein conformational changes from single cells to whole organisms. His research aims to expand the diagnostic and mechanistic understanding of protein misfolding in complex biological systems. Before transitioning to proteomics, Dr. Bamberger was recognized for his contributions to the discovery and characterization of the p53-like tumor suppressor transcription factor p63. He also played a key role in elucidating the interactome of the ΔF508 mutant of the cystic fibrosis transmembrane conductance regulator (CFTR), a common mutation linked to cystic fibrosis. His current work continues to push the boundaries of mass spectrometry-based assays for the detection and quantification of pathological protein misfolds in both cancer and neurodegenerative diseases.

Accurate Quantification of Protein Conformations with the Isotope Label-based Bottom-up Proteomics Approach 'Covalent Protein Painting'

This seminar will introduce covalent protein painting (CPP), a stable isotope-based protein footprinting technology designed to detect and quantify protein conformational changes using bottom-up mass spectrometry. CPP leverages a rapid, site-specific chemical modification of lysine residues with dimethyl labels to assess the structural accessibility of proteins in complex biological samples, including cells, tissues, and whole organisms. We will present the underlying principles of CPP, discuss experimental workflows, and explore data analysis strategies in detail. Through selected case studies, we will demonstrate the utility of CPP in probing conformational dynamics associated with cancer, neurodegeneration, and protein misfolding disorders such as cystic fibrosis. The seminar will highlight how CPP enables quantitative insights into disease-relevant structural changes at the proteome level.

During this talk you will learn about:

• We will provide insight into the protein footprinting technology Covalent Protein Painting.
• Attendees will hear about successful experiment design with Covalent Protein Painting.
• We will cover the interpretation of stable isotope labels in Covalent Protein Painting with regards to protein structure.

Biographies and Abstracts – Nuclear Magnetic Resonance

Jeanine Prompers, PhD | Professor
Department of Human Biology
Institute of Nutrition and Translational Research in Metabolism
Maastricht University Medical Centre (Netherlands)

Prof. Dr. Prompers is professor of Organ-Specific Metabolic Imaging in the Department of Human Biology at the NUTRIM Institute of Nutrition and Translational Research in Metabolism of Maastricht University Medical Centre. Her research focuses on the development of multi-nuclear MRS and MRI methods for the in vivo study of tissue metabolism in metabolic diseases. She has a strong track record on the application of ultra-high field MRS to measure energy and lipid metabolism in skeletal muscle, liver and heart, in particular in the setting of obesity-related diseases. She is one of the pioneers of deuterium metabolic imaging and was the first to perform this technique in human brain and liver at ultra-high field. Since 2024, Prof. Prompers is also CEO of Scannexus, the ultra-high field MRI facility on the Brightlands campus in Maastricht. Prof. Prompers has published over 90 papers and has supervised 15 PhD students as (co-)promotor.

Advances in Deuterium Metabolic Imaging: Paving the Way to Clinical Translation

Deuterium (2H) magnetic resonance spectroscopy (MRS) and spectroscopic imaging (i.e., deuterium metabolic imaging; DMI) provide powerful, non-invasive means to study tissue metabolism in vivo. In particular, DMI enables real-time tracking of metabolic conversions such as the transformation of deuterated glucose into lactate, offering direct insights into altered metabolic pathways like the Warburg effect in tumors. This lecture will highlight recent advances in deuterium metabolic imaging in humans, particularly at ultra-high magnetic field strengths. Examples from both healthy volunteers and patient studies will illustrate the clinical potential of this emerging technique.

During this talk you will learn about:

• Understand the principles and methodology of deuterium metabolic imaging (DMI), including how deuterated substrates are used to trace metabolic pathways in vivo.
• Learn about the advantages and challenges of performing DMI in humans at ultra-high magnetic field strengths, and how these impact sensitivity and spatial resolution.
• Gain insight into emerging clinical applications of DMI, with examples demonstrating how this technique can reveal altered metabolism in disease, such as cancer.

Haribabu Arthanari, PhD | Associate Professor
Biological Chemistry and Molecular Pharmacology
Harvard Medical School and Dana-Farber Cancer Institute (USA)

Title and Abstract TBA

During this talk you will learn about:

• TBA

Yaqiang Wang, PhD | Assistant Professor
Department of Biophysics
Medical College of Wisconsin (USA)

Dr. Yaqiang Wang is an Assistant Professor in the Departments of Biophysics and Obstetrics & Gynecology at the Medical College of Wisconsin. He earned his Ph.D. in Biochemistry from the University of North Carolina at Chapel Hill under the mentorship of Dr. Gary Pielak and completed his postdoctoral training with Dr. Juli Feigon at UCLA. He later served as Principal Scientist at Arrakis Therapeutics, where he led structural biology initiatives in RNA-targeted small-molecule drug discovery. Dr. Wang’s research centers on uncovering the structural and mechanistic principles of oncogenic noncoding RNAs and their recognition by proteins and small molecules. His laboratory employs an integrated toolkit—including NMR spectroscopy, cryoEM, X-ray crystallography, and biochemical assays—to visualize RNA and ribonucleoprotein complexes, with the goal of advancing RNA-targeted therapeutic development.

Isotopic Labeling Strategies for RNA-Targeted Drug Discovery

RNA has emerged as a promising therapeutic target, driven by growing insights into its diverse biological roles. Structural studies of RNA and RNA–protein complexes are essential for elucidating molecular recognition mechanisms and advancing RNA-targeted drug discovery. Isotopic labeling enables atomic-resolution characterization of RNA structure, dynamics, and ligand interactions, particularly through NMR spectroscopy. In this presentation, I will explore isotopic labeling strategies for RNA in the context of drug discovery, addressing the unique challenges of RNA-targeted therapeutics, comparing labeling approaches, and highlighting practical considerations for their implementation.

During this talk you will learn about:

• Understand how isotopic labeling enhances structural studies of RNA and RNA–ligand complexes.
• Evaluate different RNA labeling strategies for NMR and complementary structural techniques.
• Design labeling strategies that optimize experimental outcomes while balancing cost and project timelines in drug discovery pipelines.

Yves Aubin, PhD | Research Scientist
Regulatory Research Division, Biologics and Radiopharmaceutical Drug Directorate
Health Canada (Canada)

Dr. Aubin obtained his PhD in biophysical chemistry at Yale University and carried out post-doctoral studies at the University of Toronto and The Hospital for Sick Children in Toronto. After he moved to the Merck Research Laboratories in Montreal, where he applied NMR spectroscopy to the studies of enzyme-inhibitor interactions in support of medicinal chemistry. He then took a research scientist position at Health Canada where he developed a research program in the characterization of protein structure of recombinant protein therapeutics. His laboratory is specialized in the production of isotope-labeled proteins from E. coli and Pichia pastoris in order to apply multi-dimensional NMR methods. This lays the basis for the development of analytical methods for the assessment of higher order structure of biotherapeutics and the study of excipient-drug interactions.

Protocol for the Preparation of Fab and Fc Fragments from Therapeutic Monoclonal Antibodies Using Escherichia coli to Speed up Complete Backbone and Near-complete Side-chain Methyl Assignment

Characterization of therapeutic monoclonal antibodies (mAbs) using NMR spectroscopy has benefited from recent advances in sample preparation methods for isotopically labeled fragments. These have opened new possibilities for method development for the detailed assessment of the structure of innovator and biosimilar products, the study mAb-excipients interactions using protein dynamics, and others. Here, we propose a simple protocol that facilitates and accelerates the resonance assignment step that is required to fully exploit the strengths of NMR spectroscopy. The proposed approach is based on a simplified version of our single chain strategy, where the heavy and the light chains are produced separately in E. coli and mixed together prior to refolding. This offers the advantage of performing differential labelling where only one chain (either the heavy or the light) is isotopically labelled, thereby providing simpler NMR spectra that are straightforward to analyze and assign by NMR, either by computer-assisted manual assignment, or fully automatic assignment software packages. The protocol was demonstrated on bevacizumab, infliximab, rituximab, and trastuzumab monoclonal antibodies. Near complete assignments (>90%) of the backbone resonance of bevacizumab was accomplished in only a few hours. Moreover, use of ¹³C-glucose while allowing comparable results in terms of backbone assignment completeness, also allowed near complete assignments of side-chain methyl groups of alanine, threonine-γ1 and isoleucine-γ2.

During this talk you will learn about:

• Antibody fragments Fab and Fc can be economically prepared and allow complete NMR characterization
• Complete resonance assignment is greatly facilitated and available to the non-expert
• NMR studies of antibodies is now straightforward

 Biographies and Abstracts – Environmental

Rebecca Weed, PhD | Research Scholar
North Carolina State University (USA)

Dirty Water, Clean Data: How We Measure and Detect PFAS Using Stable Isotope Standards

Abstract TBA

During this talk you will learn about:

• TBA

Adrian Covaci, PhD | Professor
Department of Pharmaceutical Sciences
University of Antwerp (Belgium)

Prof. Dr. Adrian COVACI (53 y) is currently a professor of Environmental Toxicology and Chemistry at the University of Antwerp, Belgium. He is the current director of the Toxicological Center in the Department of Pharmaceutical Sciences. After he has acquired a PhD in Chemistry in 2002, he became a full professor in 2012. Current fields of interest are the “application of advanced mass spectrometric techniques to the human exposome,” “human biomonitoring of emerging contaminants,” and “metabolomics and human metabolism of xenobiotics in in vitro and in vivo systems.” He has co-authored more than 850 articles in peer-reviewed journals and has an H-index of 105. His papers have been cited more than 42,000 times which has earned him the title of Highly Cited Researcher for nine consecutive years between 2015 and 2023. He is the Belgian representative in the Division of Chemistry in the Environment of the European Chemical Society (EuCheMS), since 2011 and a member of the Belgian Health Council since 2022. He is also co-editor-in-chief for Environment International (IF2023: 10.3) was between 2012 and 2022 an associate editor for Science of the Total Environment (IF2023: 8.4).

Ion Mobility Spectrometry of Quaternary Ammonium Disinfectants

Collision cross section (CCS) values derived from ion mobility high-resolution mass spectrometry (IM-HRMS) can serve as an additional identification parameter in suspect and non-target screening analyses of contaminants of emerging concern (CECs), such as quaternary ammonium compounds (QACs). We present the advantages of using CCS-m/z trendlines (i.e., the relationship between CCS values and mass-to-charge (m/z) ratios) for the annotation of suspect QACs. Indoor dust samples (n=46) from Flanders (Belgium) were extracted and analysed by liquid chromatography (LC) coupled to IM-HRMS. QACs were identified as two relevant contaminant classes, with several compounds showing high abundances and detection frequencies. Twenty-one QACs were identified at confidence level (CL) 1[2] and another 17 QACs could be assigned to CL 3, as no library mass spectra were available and/or possible isomeric structures could not be narrowed down to a single candidate. Therefore, CCS values for the assigned suspects were matched against m/z-CCS trendlines established for QACs for which reference standards were available, respectively[3]. This approach allowed the identification of extensive homologue series for both classes containing structural modifications barely described in literature so far. For QACs, in contrast to available standards, homologues with uneven numbered side chains were identified. For all suspect QACs, experimental CCS values fell within the 95th percent confidence interval calculated for the reference CCS-m/z trendlines, vastly contributing to the confidence in the compound annotation. References: [1] Belova, L., Celma, A., et al., Anal Chim Acta, 2022; 1229: 340361. [2] Schymanski, E L, Jeon J, Gulde R et al., Environ Sci Technol, 2014; 48(4): 2097-8. [3] Belova, L., Caballero-Casero, N., et al., Anal Chem, 2021; 93(16): 6428-6436.

During this talk you will learn about:

• Ion mobility principles and applications
• Identification of new QACs in indoor dust samples

Shoji Nakayama, MD, PhD | Deputy Director
Japan Environment and Children's Study Programme Office (Japan)

Dr. Shoji Nakayama holds MD and PhD degrees. He is certified as public health specialist/supervisor by Japan Board of Public Health and Social Medicine. He serves as associate editor of Environment International as well as Journal of Exposure Science and Environmental Epidemiology. In 2005, Dr. Nakayama was invited by the US Environmental Protection Agency and spent six years to conduct exposure research on contaminants of emerging concern. In 2011, Dr. Nakayama joined the National Institute for Environmental Studies in Japan. Currently he is deputy director of the Japan Environment and Children’s Study Programme Office. He also holds a professor title at the St. Luke’s International University, the University of Tsukuba and Icahn School of Medicine at Mount Sinai. Dr. Nakayama is a lead exposure scientist for the Japan Environment and Children’s Study (JECS), which is a longitudinal birth cohort study involving 100,000 mothers and children. He is devoted to human biomonitoring research. Exposome research is his most recent activity. He collaborates with US, Canada, EU and Asian researchers to advance and promote children’s environmental health.

Children's Environmental Epidemiology and Human Biomonitoring in Japan

Recent environmental health research including epidemiological studies have focused on the impact of chemical exposure on children’s health and development. Japan has been conducting a large-scale birth cohort study, involving >100,000 mother-child pairs, since 2011, namely the Japan Environment and Children's Study (JECS). Along side the longitudinal study, the Ministry of the Environment, Japan launched a nationwide human biomonitoring (HBM) program this year. In this presentation, the outcomes and future of JECS as well as details about ongoing HBM will be introduced.