The annual Al Yergey Mass Spectrometry Scientist Award, established in 2018, continues to commemorate the profound legacy of its namesake, a revered figure whose dedication to mentorship, innovation, and public service left an indelible mark on the mass spectrometry (MS) field. Inaugurated on the 50th anniversary of Yergey’s ASMS membership and coinciding with the year of his passing, the award annually recognizes three individuals who have not only propelled mass spectrometry forward through groundbreaking work but have also exemplified Al Yergey’s unwavering commitment to fostering the growth and success of others throughout their careers. This year, the scientific community gathered at the American Society for Mass Spectrometry (ASMS) conference to celebrate the achievements of the 2026 honorees: Daniel McClatchy, Michael Senko, and Kevin Giles. Their contributions span critical areas from novel biological labeling techniques to transformative instrument design, collectively illustrating the dynamic evolution and expanding capabilities of mass spectrometry.
The Enduring Legacy of Al Yergey and the Award’s Genesis
Al Yergey, often remembered as an unsung hero of mass spectrometry, was more than just a scientist; he was a pillar of the community. His career was characterized by a rare blend of scientific ingenuity, a profound commitment to mentoring aspiring researchers, and dedicated public service. He was known for his generous spirit, always willing to share knowledge and lift up those around him. The Al Yergey Mass Spectrometry Scientist Award was conceived as a living tribute to these very qualities, ensuring that his ethos of collaborative progress and human-centric scientific development continues to inspire future generations. The selection criteria for the award deliberately mirror Yergey’s values, seeking individuals who not only innovate at the forefront of MS but also actively engage in nurturing talent and building a stronger scientific community. The ASMS, as the premier professional organization for mass spectrometry, serves as the ideal platform for this recognition, bringing together a global network of scientists, technologists, and industry leaders who benefit from and contribute to the advancements in the field. Since its inception, the award has highlighted a diverse group of scientists, reinforcing the multifaceted nature of progress in mass spectrometry, from fundamental research to applied technologies.
Daniel McClatchy: Illuminating Proteomic Dynamics in Neuroscience
Among this year’s distinguished recipients is Daniel McClatchy, a Senior Staff Scientist in the esteemed Yates lab at the Scripps Research Institute in California, USA. McClatchy’s work centers on the critical area of quantitative method development, specifically tailored for investigating complex neuroscience disease models. His recognition stems largely from his pioneering efforts in developing techniques that allow for unprecedented insights into proteome dynamics in vivo.
A significant breakthrough attributed to McClatchy is the development of the Pulse Azidohomoalanine Labeling in Mammals (PALM) method. This innovative technique allows for the in vivo labeling of rodent proteomes, providing a window into the most dynamic aspects of cellular life. PALM builds upon foundational work by scientists like Dave Tirell and Erin Schuman at the California Institute of Technology, who developed non-canonical amino acids such as Azidohomoalanine (AHA) and, more recently, Azidonorleucine (ANL). In the PALM methodology, AHA is metabolically incorporated into newly synthesized proteins in place of methionine. This strategic substitution enables subsequent "click chemistry" reactions, allowing for the enrichment of these newly formed proteins from the broader proteome. The ability to isolate and analyze newly synthesized proteins is crucial because this fraction of the proteome undergoes the most rapid and significant changes, particularly in the context of disease. By focusing on this dynamic subset, researchers can gain a much clearer understanding of cellular processes, track disease progression, and potentially identify novel biomarkers with greater precision.
McClatchy acknowledges that PALM’s full potential is still unfolding, particularly with the advent of cell-specific compounds like ANL. While AHA enabled the study of the entire brain proteome, ANL promises to revolutionize neuroscience research by allowing the labeling of specific cell types within the brain. This targeted approach is profoundly important in neuroscience, where understanding the unique contributions and dysfunctions of particular neuronal or glial populations in disease states is paramount. McClatchy’s ongoing work aims to leverage this specificity to unravel the intricate proteomic changes occurring in distinct cell types, thereby advancing the understanding and treatment of neurological disorders.
For researchers contemplating the adoption of PALM, McClatchy offers invaluable advice, particularly regarding downstream analysis. He highlights two primary approaches: protein enrichment and peptide enrichment, each with distinct advantages and disadvantages. Historically, protein enrichment has been the more common method, involving a click reaction to attach biotin, followed by pull-down with streptavidin. However, a significant challenge with this approach is the infrequent detection of the biotin tag post-digestion, raising concerns about potential non-specific protein co-enrichment. McClatchy’s team pioneered an alternative: performing protein digestion first, then enriching biotin-tagged peptides. This method offers 100% certainty that identified peptides originate from newly synthesized proteins. The trade-off, however, is reduced sensitivity, as detection relies on fewer tagged peptides. McClatchy’s group is actively engaged in refining this pipeline to enhance its sensitivity, making this highly specific method more widely applicable.
Beyond PALM, McClatchy also played a pivotal role in optimizing Stable Isotope Labeling of Mammals (SILAM) for quantitative in vivo proteomics. SILAM is a powerful quantitative technique that involves labeling entire mouse or rat proteomes with heavy N15 isotopes. This is achieved by feeding the animals a specialized diet where spirulina, a blue-green algae 100% labeled with N15, is the sole protein source. While SILAM was initially developed in John Yates’s lab by Christine Wu and Mike MacCoss, McClatchy’s contributions were instrumental in refining its practical application. He focused on the intricate details of the workflow, particularly determining the precise duration required to achieve 100% labeling in various tissues and under different experimental conditions. Achieving complete labeling can be a lengthy process, often taking months or even generations, necessitating careful planning and execution.
McClatchy underscores the versatility of SILAM, noting its evolving applications. Initially employed primarily for quantifying proteomic differences between diseased and non-diseased states, SILAM is now being leveraged to investigate protein longevity and turnover. Researchers can label animals, transition them to a regular diet, and then monitor the degradation rates of various proteins over time, providing crucial insights into protein half-lives and dynamic cellular processes. A key piece of advice for new SILAM users is the critical importance of robust bioinformatic tools, given the complexity of calculating N15 incorporation rates. Furthermore, McClatchy highlights a nuanced but important consideration: the introduction of heavy stable isotopes can subtly alter the proteome. While not drastic, these changes necessitate careful experimental design and the consistent use of appropriate controls, such as internal standards, to ensure the validity and interpretability of results. For McClatchy, receiving the Al Yergey Award is a profound honor, placing him among a cadre of "really amazing scientists" whose accomplishments he deeply respects.
Michael Senko: Engineering the Future of Mass Spectrometry Instrumentation
Michael Senko, a Principal Scientist at Thermo Fisher Scientific in Massachusetts, USA, is another deserving recipient, recognized for his three decades of tireless work in advancing mass spectrometry instrumentation. His career has been defined by a relentless pursuit of improved instrument performance and the development of new analytical capabilities, enabling scientists across proteomics, biopharmaceutical characterization, and life science research to tackle increasingly complex biological questions.
Senko expresses immense pride in his career, which has seen the development of pioneering benchtop ion traps evolve into high-performance hybrid mass spectrometers boasting industry-leading resolution. These innovations have dramatically expanded the speed, sensitivity, flexibility, and analytical power of mass spectrometry. However, he emphasizes that these achievements are not his alone but the result of building and collaborating with exceptional teams of scientists and engineers whose collective creativity and dedication made these advancements possible.
Among his many contributions, Senko is particularly proud of his role in developing the original Linear Trap Quadrupole (LTQ). This groundbreaking instrument simultaneously enhanced sensitivity, dynamic range, and scan speed compared to earlier 3D ion traps. The LTQ’s ability to achieve this trifecta of improvements fundamentally transformed tandem mass spectrometry, laying a robust foundation for numerous subsequent advances in the field. Equally significant is his contribution to creating the Tribrid architecture, a revolutionary design that integrates a quadrupole, an ion trap, and an Orbitrap into a single instrument. This unique combination offers unparalleled flexibility, allowing scientists to select the optimal mass analysis and fragmentation methods for each specific experiment. For Senko, the greatest satisfaction comes from witnessing researchers present their discoveries at ASMS, knowing that these breakthroughs would have been impossible without the instruments he helped to create.
For those new to the sophisticated Tribrid mass spectrometers, on which Senko has served as technical lead for over a decade, he offers practical advice. First, he cautions against the temptation to immediately utilize every feature. Instead, he recommends starting with simpler experiments and gradually introducing complexity as users gain familiarity with the contributions of each analyzer and fragmentation method. Second, he advises letting the scientific question dictate the method, rather than allowing the instrument’s capabilities to constrain the research focus. Finally, and perhaps most crucially, Senko stresses the paramount importance of investing in meticulous sample preparation and experimental design. Even the most advanced instrument can only reveal the information present in a high-quality sample.
Receiving the Al Yergey Award holds profound personal meaning for Senko. He values the recognition from the mass spectrometry community and the honor of being associated with Al Yergey’s enduring legacy. He recounts a personal connection, noting that Al’s younger brother, Jim Yergey, served as his guide during some of his earliest ASMS meetings. This personal link makes the award bearing the Yergey name particularly special. Senko views the award not merely as an acknowledgment of past accomplishments but as a powerful reminder of the continuous importance of community, collaboration, and relentless innovation in pushing the boundaries of scientific discovery.
Kevin Giles: Master Architect of Ion Optics and Ion Mobility-MS
The third esteemed recipient of the Al Yergey Mass Spectrometry Scientist Award is Kevin Giles, who recently retired from Waters Corporation in Massachusetts, USA. While the opportunity to directly interview Mr. Giles was missed as he enjoys a well-deserved retirement, his profound impact on mass spectrometry instrumentation is widely recognized and celebrated by the American Society for Mass Spectrometry.
Giles is lauded for his extensive contributions to the design, refinement, and commercialization of advanced mass spectrometry systems, with a particular focus on ion optics development. His work profoundly influenced the efficiency and performance of MS instruments. Key innovations include the design and implementation of RF-confining stacked-ring ion guides and travelling wave technology. These technologies are now integral components in a significant proportion of Waters’ mass spectrometry instruments, including the widely used StepWave source ion guide, which dramatically enhances ion transmission and sensitivity.
Perhaps Giles’ most significant and transformative contribution lies in his work on ion mobility-mass spectrometry (IM-MS) instrumentation. His efforts were central to bringing IM-MS from a specialized research technique into mainstream analytical science. He played a pivotal role in the development of the Synapt Q-ToF series, instruments that were instrumental in establishing IM-MS as a practical and powerful tool for a broad range of applications. A cornerstone technology within the Synapt instruments is the novel Travelling Wave Ion Mobility separation device, which Giles was instrumental in developing and optimizing. This culminated in the design and commercialization of an exceptionally versatile cyclic IM-MS instrument, further expanding the capabilities of IM-MS for separating complex mixtures and providing additional dimensions of analytical information.
In his final years at Waters, Giles continued to push the boundaries of MS technology, leading the design and implementation of the first dedicated commercial Charge Detection MS instrument. This cutting-edge project, undertaken in collaboration with Indiana University, represents a significant leap forward in analyzing large biomolecules and nanoparticles, opening new avenues for research in areas like gene therapy and virology. Kevin Giles’ career is a testament to the power of engineering innovation in translating complex scientific principles into robust, commercially viable tools that empower researchers worldwide. His contributions have irrevocably shaped how mass spectrometry is performed, making advanced analytical capabilities accessible to a broader scientific community.
Broader Impact and Future Implications of Mass Spectrometry
The collective achievements of Daniel McClatchy, Michael Senko, and Kevin Giles underscore the vibrant and rapidly evolving landscape of mass spectrometry. Their pioneering work, recognized by the Al Yergey Award, exemplifies how synergistic advancements in both methodology and instrumentation are crucial for pushing the boundaries of scientific discovery.
McClatchy’s innovations in PALM and SILAM directly address the critical need for more dynamic and precise proteomic analyses, particularly in complex biological systems like the brain. The ability to track newly synthesized proteins or quantify protein turnover in vivo provides unprecedented insights into disease mechanisms, biomarker discovery, and therapeutic efficacy. As neuroscience continues its quest to unravel the complexities of neurological disorders, techniques that offer cell-specific and temporal resolution will be indispensable. These methods promise to accelerate the identification of therapeutic targets and the development of personalized medicine approaches.
Senko’s relentless pursuit of enhanced MS instrumentation, from the foundational LTQ to the sophisticated Tribrid architecture, has fundamentally reshaped what is possible in mass spectrometry. Improved sensitivity, speed, and analytical versatility are not merely technical feats; they are enablers of entirely new scientific questions. Researchers can now characterize biomolecules with unparalleled detail, analyze complex mixtures in shorter times, and perform experiments that were previously unimaginable. These instrumental advances are vital for fields ranging from biopharmaceutical development (e.g., characterizing complex protein therapeutics) to environmental monitoring and fundamental biological research, providing the robust tools necessary to address the grand challenges of our era.
Giles’s profound contributions to ion optics and ion mobility-mass spectrometry have made sophisticated separation techniques more accessible and powerful. His work on travelling wave technology and the Synapt Q-ToF series transformed IM-MS from a niche research tool into a mainstream analytical staple. Ion mobility adds an extra dimension of separation based on molecular shape and size, which is critical for resolving isomers, characterizing protein conformations, and analyzing complex biological mixtures with greater confidence. The commercialization of Charge Detection MS further exemplifies his forward-thinking approach, pushing the limits of what MS can analyze, particularly for very large or heterogeneous samples.
Collectively, these award winners represent the harmonious interplay between methodological innovation and instrumental engineering that defines progress in mass spectrometry. Their work not only provides powerful new tools but also inspires the next generation of scientists to explore uncharted territories. The legacy of Al Yergey, characterized by innovation and mentorship, continues to thrive through these individuals, fostering a scientific environment where groundbreaking discoveries are not only made but also shared and propagated. As mass spectrometry continues its rapid evolution, driven by such dedicated individuals, its impact on human health, environmental science, and fundamental biological understanding is poised to grow exponentially, promising a future of increasingly precise and insightful scientific exploration.
