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Many pharmacology experiments produce beautifully clean assay curves. Potency estimates appear precise, maximal responses align neatly, and screening data generates clear rank orderings of compounds. The harder question is what those assay signals actually predict biologically. Drug discovery programs rarely fail because an assay produced poor data. They fail because the interpretation of that data did not translate to biology outside the assay system . Pharmacology exists precisely to bridge that gap. It creates conceptual scales that allow scientists to project observations from one experimental system into another. During a recent AMA discussion, several experienced scientists raised questions about assay scaling, pharmacokinetics, and discovery decision-making. Dr. Kenakin used those questions to explore how pharmacological reasoning turns experimental signals into actionable insight. In this session, you’ll gain: How pharmacology translates assay signals into biological predictions Why EC₅₀ values rarely capture the full pharmacological picture How binding kinetics and PK considerations influence discovery decisions Drug Discovery Pharmacology Principles in Action Drug discovery pharmacology principles revolve around one core idea: translation . Chemistry identifies molecules. Biology reveals targets. But pharmacology asks a different question: How will this molecule behave in a system we have not yet tested? That predictive step is essential because discovery scientists almost always operate inside partial models  of biology. Key realities pharmacologists face: Assays measure one slice of biology Disease physiology involves many interconnected systems Drug concentrations constantly rise and fall in vivo Pharmacology therefore constructs conceptual scales—linking ligand binding, receptor activation, and downstream signaling—to project how molecules behave beyond the assay. As Dr. Kenakin explains, pharmacology differs from other life sciences precisely because it builds quantitative frameworks that allow projection from one system to another.   The Assay Window Problem Every functional assay operates within a measurement window , and interpreting results requires understanding how responses scale within that window. Consider calcium flux assays: Teams often ask how to define fractional receptor activation, similar to how forskolin establishes maximal cAMP signaling. Practical strategies include: Using known controls (e.g., ATP or carbachol) to define maximal signal Normalizing agonist responses to a common reference window Accepting that maximal response may be estimated rather than exact In practice, the precise maximal signal matters less than many assume. When responses are scaled consistently, comparisons remain meaningful even if the absolute maximum is imperfect. As Dr. Kenakin notes, much of the interpretive power comes from the EC₅₀ component of the response , while small differences in maximal signal contribute relatively little to the overall interpretation. EC₅₀ Misconceptions Persist Few misunderstandings derail discovery programs faster than misinterpreting EC₅₀. Even experienced biologists sometimes treat EC₅₀ as if it reflects ligand affinity. In reality, it represents something very different: EC₅₀ is a system-dependent measure of functional response. It reflects: receptor density signaling efficiency assay sensitivity downstream amplification Not simply ligand binding. This distinction becomes especially important when comparing mutants, partial agonists, or signaling pathways. A ligand may show identical EC₅₀ values in two assays while engaging receptors through very different mechanisms. Understanding this distinction allows teams to: interpret pharmacological differences across systems normalize mutant receptor data avoid misleading potency comparisons Dr. Kenakin reveals how scaled pharmacological metrics allow teams to interpret receptor signaling changes even when expression levels vary. Time Matters More Than Potency For decades, discovery teams prioritized potency above all else. The logic seemed obvious: Higher potency → lower dose → fewer side effects. But this assumption misses a crucial pharmacological reality: biological systems operate in time, not equilibrium. Drug concentrations constantly change as molecules: distribute through tissues bind and unbind receptors undergo metabolism and clearance This dynamic environment makes residence time —how long a ligand stays bound to its receptor—critically important. Two compounds with identical potency may behave very differently in vivo if one remains bound longer. Dr. Kenakin highlights that therapeutic efficacy depends on the period during which a drug is actively engaged with its target , not simply how strongly it binds at equilibrium. When PK Ends Programs Discovery teams often fall in love with molecules that show beautiful activity in vitro. But pharmacology introduces a sobering truth: A drug that cannot reach its target is not a drug. Pharmacokinetics—absorption, distribution, metabolism, and excretion—must therefore be addressed early. Common PK deal breakers include: poor solubility preventing absorption rapid clearance eliminating exposure sequestration in tissues or proteins One classic example occurs when compounds dissolve poorly, behaving essentially like inert particles within biological systems. Even potent inhibitors may fail simply because they never reach sufficient concentration in vivo . The good news is that modern technologies—from delivery systems to alternative dosing routes—are dramatically expanding the options available to rescue promising scaffolds. Dr. Kenakin discusses how discovery teams balance enthusiasm for biological activity with the practical constraints of pharmacokinetics. Chemists Make The Drugs Drug discovery is fundamentally a team sport . Pharmacologists interpret biological data. But chemists transform that data into molecules capable of becoming medicines. Kenakin often recalls advice from Nobel laureate James Black: Chemists make the drugs. Your job as a pharmacologist is to guide them with solid data. This relationship defines productive discovery teams. Pharmacologists contribute: rigorous assay interpretation mechanistic insight into receptor signaling quantitative frameworks for decision making Chemists contribute: structural creativity scaffold optimization elimination of toxic chemical features Experienced chemists, for example, instinctively avoid known toxicophores —chemical groups associated with safety liabilities. When both disciplines collaborate effectively, pharmacology data becomes a roadmap that guides molecular design toward viable drug candidates. Failure Is the Real Curriculum Drug discovery carries a difficult truth: most programs fail. Even promising molecules collapse due to safety issues, pharmacokinetics, or unexpected biology. Yet failure is not a sign of weakness in discovery science. It is the mechanism by which progress occurs. Kenakin summarizes the mindset required with a quote attributed to Winston Churchill: Success is the ability to go from failure to failure without loss of enthusiasm. For scientists entering drug discovery, the lesson is simple: most hypotheses will be wrong most compounds will fail persistence is essential But the iterative process—assay, interpretation, redesign—ultimately produces the breakthroughs that transform medicine.Dr. Kenaking reveals how experienced pharmacologists turn repeated failures into increasingly powerful insights. Why Terry’s Corner Drug discovery pharmacology principles rarely appear in textbooks the way they are practiced in industry. Terry’s Corner  was created to close that gap. Subscribers gain access to: Weekly pharmacology lectures by Dr. Terry Kenakin Monthly live AMAs with real discovery questions A growing on-demand library of practical pharmacology insights The Corner is built for: pharmacologists refining core analytical tools discovery teams navigating development bottlenecks scientific leaders seeking clear pharmacological guidance GPCR innovation is accelerating rapidly. The scientists who strengthen their pharmacology foundations today will define tomorrow’s breakthroughs. Explore the full library and trailers ➤ https://www.ecosystem.drgpcr.com/terry-corner

The A2A adenosine receptor (A2AAR) is one of four adenosine receptor subtypes expressed in the human body (A1, A2A, A2B, and A3). It plays a key role in immune system downregulation, making it an attractive target for conditions in which immune reactivation is desired. A2AAR-targeted therapies have advanced to phase II clinical trials for various cancers, particularly in combination with other immune checkpoint inhibitors.1 In a shared effort to develop robust screening approaches  that can serve as practical alternatives to radioligand binding assays, Celtarys Research and PROMEGA combined their respective technologies to support GPCR drug discovery. A new NanoBRET® competitive binding assay 2  was developed in collaboration with Professor Kevin Pfleger’s laboratory (University of Western Australia), using a new Celtarys fluorescent ligand. Figure 1. Scheme of a competitive NanoBRET® assay. GPCRs are part of Celtarys’ expertise fields. Using a similar pharmacophore  to the one present in the A 2A AR probe CELT-300 , new fluorescent ligands adapted to the NanoBRET® technology were designed and synthesized. The Nanobret® 590 Dye  commercialized by PROMEGA was used as the fluorophore tag . The competitive assay design and optimization were performed in the University of Western Australia. GPCRs are part of Celtarys’ expertise fields. Using a similar pharmacophore  to the one present in the A 2A AR probe CELT-300 , new fluorescent ligands adapted to the NanoBRET® technology were designed and synthesized. The Nanobret® 590 Dye  commercialized by PROMEGA was used as the fluorophore tag . The competitive assay design and optimization were performed in the University of Western Australia. Combining Two Technologies Into One to Measure A2A Fluorescent Competitive Binding Bioluminescence resonance energy transfer  (BRET) serves as the basis for the NanoBRET® Target Engagement (TE) Technology. In this proximity-based approach, a NanoLuc®luciferase   genetically fused  to the target protein   transfers  bioluminescence to a fluorescent   tracer  binding to the target protein. In the competitive assay, A 2A AR ligands are set to compete with the probe , and the interactions  between the ligands and protein are quantified in real time  by measuring the probe’s emission in intact cells. To synthesize the probe, Celtarys has applied its proprietary conjugation technology . First the fluorescent ligand is properly functionalized to keep its activity intact. Then, the linker composition is optimized, by using different hinges and spacers . Afterwards, the fluorophore is attached and the final probes evaluated.  Celtarys’ technology significantly reduces the time it takes to obtain fluorescent tags and test varying linker structures and lengths, and it was used here to ensure optimal performance in NanoBRET® TE assays. Results The combination of both technologies, and the expertise of Prof. Pfleger’s group in developing assays, led to two new A 2A AR tracers (CELT-463 and CELT-464) , bearing the same pharmacophore and fluorophore, but with different linkers. They can be used to verify target engagement  and calculate ligand affinity  in a NanoBRET ®-based competitive binding assay .  Saturation binding experiments on NanoLuc®-tagged A2A receptors. First, saturation binding assays were performed . They are needed to identify the best concentrations for each tool. The curves obtained were consistent, and high specific binding  and optimal signal to noise rat io were observed. Figure 2 . Saturation Binding Experiment for CELT-463 (KD=33±4nM) and CELT-464 (KD=44±5nM) using HEK293FT cells transiently transfected with signal peptide nanoluc®-A2AAR expression vector.  Transfected cells were treated with increasing concentrations of CELT-463 or CELT-464 in the presence (non-specific binding) or absence (total binding) of SCH 442416. Specific binding was calculated by subtracting non-specific binding from total binding (mean±SEM, n=6). NanoBRET® competitive binding assays on A2AAR with CELT-463 and CELT-464 Using the previous data as reference, 50nM was chosen as the tracer concentration  for the assays, as it produces a sufficiently large window to perform the experiment. Increasing concentrations of the competitor compounds were added and the signal measured. As seen in figure 2, a heterogenous set of compounds  (agonists and antagonists, different structures) was measured using both CELT-463  and CELT-464 . Figure 3. Measurement of competitive ligand binding to A2AAR using tracers CELT-463 and CELT-464 in NanoBRET® assays for a set of reference compounds. Cells expressing signal peptide-nanoluc®-A2AAR were treated with 50nM CELT-463 or CELT-464 in the presence of increasing concentrations of various competitor compounds (mean±SEM, n=6). Selective or promiscuous, agonists or antagonists were for all 4 Adenosine Receptors were included in this set. the data obtained were compared with those reported in literature, which were obtained employing radioligand binding assays. Table 1. Set of reference compounds tested for assay validation, together with the reported and experimental binding data. PKI values were derived from pIC50 values using the Cheng-Prusoff equation. 3 The pK i values display a similar order  of affinity to the reported values , guaranteeing the NanoBRET® competitive binding assay on A 2A AR, meaning CELT-463  and CELT-464  are a valid alternative  to radioligand binding and other traditional methodologies. Conclusions This collaboration between PROMEGA, Celtarys Research, and the University of Western Australia led to the identification of two fluorescent ligands, CELT-463  and CELT-464 , optimized for NanoBRET®-based A2A fluorescent competitive binding affinity screening. Both are effective as NanoBRET® TE tracers, leading to similar results to those present in literature using traditional screening methods. As a proof of concept, the study shows that Celtarys’ chemistry can be translated into NanoBRET ® TE GPCR assays compatible with 384-well screening formats. For research teams, this provides a practical framework for integrating fluorescent ligand design with live-cell target engagement assays. The next step will be to determine how broadly this approach can be extended across GPCR families and how predictive these measurements are in downstream discovery workflows. Check the method to perform this assay and other case studies we have done on our website: https://www.celtarys.com/case-studies   References (1) Rodríguez-Pampín, I.; González-Pico, L.; Selas, A.; Andújar, A.; Prieto-Díaz, R.; Sotelo, E. Targeting the Adenosinergic Axis in Cancer Immunotherapy: Insights into A2A and A2B Receptors and Novel Clinical Combination Strategies. Pharmacological Reviews   2025 , 77  (6), 100092. https://doi.org/10.1016/j.pharmr.2025.100092 . (2) Stoddart, L. A.; Johnstone, E. K. M.; Wheal, A. J.; Goulding, J.; Robers, M. B.; Machleidt, T.; Wood, K. V.; Hill, S. J.; Pfleger, K. D. G. Application of BRET to Monitor Ligand Binding to GPCRs. Nature Methods   2015 , 12  (7), 661–663. https://doi.org/10.1038/nmeth.3398 .  (3) Todde, S.; Moresco, R. M.; Simonelli, P.; Baraldi, P. G.; Cacciari, B.; Spalluto, G.; Varani, K.; Monopoli, A.; Matarrese, M.; Carpinelli, A.; Magni, F.; Kienle, M. G.; Fazio, F. Design, Radiosynthesis, and Biodistribution of a New Potent and Selective Ligand for in Vivo Imaging of the Adenosine A2A Receptor System Using Positron Emission Tomography. J. Med. Chem. 2000, 43 (23), 4359–4362. https://doi.org/10.1021/jm0009843 . (4) Jacobson, K. A.; Gao, Z.; Matricon, P.; Eddy, M. T.; Carlsson, J. Adenosine A2A Receptor Antagonists: From Caffeine to Selective Non‐xanthines. British J Pharmacology 2022, 179 (14), 3496–3511. https://doi.org/10.1111/bph.15103 . (5) Borrmann, T.; Hinz, S.; Bertarelli, D. C. G.; Li, W.; Florin, N. C.; Scheiff, A. B.; Müller, C. E. 1-Alkyl-8-(Piperazine-1-Sulfonyl)Phenylxanthines: Development and Characterization of Adenosine A2B Receptor Antagonists and a New Radioligand with Subnanomolar Affinity and Subtype Specificity. J. Med. Chem. 2009, 52 (13), 3994–4006. https://doi.org/10.1021/jm900413e . (6) Klotz, K.-N. Adenosine Receptors and Their Ligands. Naunyn-Schmied. Arch. Pharmacol. 2000, 362, 382-391. https://doi.org/10.1007/s002100000315 (7) Jacobson, K. A. Introduction to Adenosine Receptors as Therapeutic Targets. In Adenosine Receptors in Health and Disease; Wilson, C. N., Mustafa, S. J., Eds.; Handbook of Experimental Pharmacology; Springer Berlin Heidelberg: Berlin, Heidelberg, 2009; Vol. 193, pp 1–24. https://doi.org/10.1007/978-3-540-89615-9_1 . (8) Yung-Chi, C.; Prusoff, W. H. Relationship between the Inhibition Constant (KI) and the Concentration of Inhibitor Which Causes 50 per Cent Inhibition (I50) of an Enzymatic Reaction. Biochemical Pharmacology   1973 , 22  (23), 3099–3108. https://doi.org/10.1016/0006-2952(73)90196-2 .

Dr. GPCR is proud to partner with the 5th Annual GPCRs-Targeted Drug Discovery Summit.  This post is your one-stop hub — agenda highlights, who's attending, our exclusive discount code, and speaker interviews as they go live. Why the GPCR Drug Discovery Field Is Converging in Boston The GPCR field is in a genuinely exciting moment. Not hype — momentum. The human genome encodes ~800 GPCRs, yet only around 15% are currently targeted by approved drugs — leaving an enormous and largely untapped therapeutic opportunity. New structural tools, AI-driven design pipelines, and a growing number of programs moving into the clinic are redefining what's possible across modalities and indications. Pharma interest is high, as reflected in major deals across the space. The 5th Annual GPCRs-Targeted Drug Discovery Summit is the industry-led meeting dedicated entirely to GPCR drug discovery — across small molecules, peptides, and antibodies, and across indications. This year's program reflects where science is actually heading. Dr. GPCR founder Dr. Yamina Berchiche will be there — if you're attending, reach out to connect. Who's at the GPCR-Targeted Drug Discovery Summit 2026 The meeting brings together 80+ senior leaders from biotech and pharma to advance GPCR programmes from discovery through translation — experts in GPCR biology, structural biology, computational design, pharmacology, and translational strategy. Companies already confirmed to attend include: Abalone Bio  ·  AbbVie  ·  Biagon  ·  Biolexis Therapeutics  ·  Confo Therapeutics  ·  Eli Lilly  ·  GSK  ·  Nabla Bio  ·  Northeastern University  ·  Nxera Pharma  ·  OMass Therapeutics  ·  Superluminal Medicines  ·  Tectonic Therapeutics  ·  and many more. GPCR Drug Discovery Agenda Highlights: What's New in 2026 This year's summit runs across three days — an AI & ML Focus Day on April 28, followed by two conference days — and the program spans the full breadth of the field. Biased Signaling, Endosomal Pathways & GPCR Signaling Complexity How do we disentangle intrinsic, system, and kinetic bias in a way that actually predicts clinical outcomes? Sessions from InterAx Biotech, Northeastern University, and Function Therapeutics dig into this — moving beyond static potency and efficacy to mechanistic signatures that guide drug design. A panel discussion will tackle best practices for measuring GPCR signaling bias in vitro and what that means for in vivo and clinical translation. AI & ML in GPCR Drug Discovery A dedicated focus day brings together teams from Nabla Bio, Abalone Bio, Biagon, Iambic Therapeutics, Lembas, and Eli Lilly. These aren't primers on AI — they're teams presenting real workflows and real data, covering generative antibody design, dynamic conformational modeling, federated computing platforms, and predictive simulations that shorten discovery timelines. Antibodies, Cyclic Peptides & Allosteric Modulators Nine or more presentations on non-small molecule approaches — including agonistic antibodies, GPCR-directed ADCs, orally available cyclic peptides, and allosteric probes for Class B GPCRs. Companies presenting include Skymab Biotherapeutics, Confo Therapeutics, GSK, Metaphore Biotechnologies, and Abilita Therapeutics. Translational Stories & Clinical Data OMass Therapeutics on long-residence MC2R antagonists. Tectonic Therapeutics on engineering a long-acting relaxin for pulmonary hypertension. Kainova Therapeutics presenting Phase 1 outcomes for their EP4 receptor antagonist in solid tumors. Alphamol on Phase 1 results from an orphan GPCR program pursued against industry skepticism. 🎥 Speaker Spotlight: GPCR Drug Discovery Experts to Watch (coming soon) In the run-up to the summit, we're speaking with some of the researchers presenting at the meeting. We'll be adding interviews here as they go live — check back for updates. Register for the GPCR Drug Discovery Summit — Exclusive DrGPCR Discount Use the exclusive DrGPCR discount code DRGPCR10 at checkout for 10% off registration. Early bird pricing also runs through March 6 , saving up to $600 off the door price — so don't wait.   🔗  Register here   🔗  Explore the full event guide   🔗  Contact the event team for your discount The 5th Annual GPCRs-Targeted Drug Discovery Summit takes place April 28–30, 2026 at The Colonnade, 120 Huntington Avenue, Boston, MA.

iPSC-derived cellular models and biosensor approaches for studying GPCR signaling and improving translational pharmacology workflows. < Back Using iPSC-derived models to study GPCR function April 16, 2026 10 AM - 11:30 AM EST 🔒 Watch Recordings Access the full library of recorded Masterclass sessions. Get Live Updates Be notified when new live Masterclasses are scheduled. Introduction Drug discovery pipelines increasingly depend on screening platforms designed to identify therapeutically valuable compounds. Yet despite advances in screening technologies, the translation of these discoveries into clinical success remains limited. A major factor is the continued reliance on cellular systems that do not adequately reflect the complexity of human tissues and disease biology. This Masterclass explores how induced pluripotent stem cell (iPSC)–derived cellular models and organoid systems can provide more physiologically relevant environments for studying GPCR signaling and pharmacological responses. The discussion will examine how these models are generated, how biosensor-based approaches can be integrated to monitor signaling pathways, and how such systems can support more translationally relevant drug discovery workflows. Instructor Terry Hébert has a long-standing track record in identifying molecular mechanisms that regulate the function of G protein-coupled receptors. His research has focused extensively on GPCR oligomerization, signaling complex assembly, and biased signaling. His current work investigates the ontogeny, formation, and trafficking of GPCR-based signaling complexes in order to understand how GPCR signaling pathways are organized and integrated within cells. This research examines signaling architecture both at the cell surface and within the nucleus, providing insight into how receptor signaling networks are structured and regulated. Upcoming Live Sessions

Discover the Dr. GPCR Ecosystem – the ultimate hub for GPCR professionals to connect, collaborate, and advance drug discovery. Home: About Accelerating GPCR Drug Discovery, Together Dr. GPCR is the global hub where academia and industry meet to advance GPCR research, accelerate drug discovery, and foster collaboration across the entire ecosystem. 👉 Join Free Today 🔒 Go Premium Strategic Partner(s) Your Path to GPCR Mastery Flexible, career-ready courses designed by scientists for scientists. 🔒 Live GPCR Masterclass ➚ 🔒 GPCR Masterclass ➚ 🔒 Terry's Corner ➚ 🔒 GPCR Weekly News ➚ Dr. GPCR Podcast ➚ Articles from the Ecosystem ➚ Drug Discovery Pharmacology Principles That Turn Assays Into Real Medicines A2A Fluorescent Competitive Binding: Advancing NanoBRET® Target Engagement for GPCR Drug Discovery GPCR Drug Discovery Summit 2026: What to Expect in Boston — and How to Register Quantifying Receptor Selectivity in Modern Drug Discovery Closing the Gap Between Academia and Industry Our vision is simple: empower the GPCR field through shared knowledge, collaboration, and open access to tools that accelerate drug discovery. 🤝 Support the Mission Home: Premium Premium Yearly $499 $ 499 Every year 🚀 Everything you need to master GPCR science — in one membership. Valid until canceled Select 🎓 Full GPCR University + 🔬 200+ expert talks 🗞️ Weekly research, careers & event intelligence 🤝 Members-only networking, AMAs & matchmaking 💡 Support open resources for the global GPCR field 🧠 Designed for researchers at every career stage 🚀 Don’t just keep up — lead the way. 🔒 Grandfather Guarantee, your rate never increases Everything You Need to Master GPCR Science in One Membership Join the most complete GPCR learning & collaboration hub. Explore the packages and choose one that works for you Advancing GPCR Science Through Collective Intelligence Dr. GPCR is a living ecosystem where global minds converge to share knowledge, spark collaboration, and shape the future of GPCR-driven discovery. 🤝 Support the Mission

Explore structure-based design of purinergic GPCR modulators with NIH scientist Kenneth A. Jacobson, covering A3 receptor agonists and P2Y14 antagonists in chronic pain. < Back Structure-Based Design of Modulators of Purinergic GPCRs Mar 12, 2026 10 AM - 12:30 PM EST 🔒 Watch Recordings Access the full library of recorded Masterclass sessions. Get Live Updates Be notified when new live Masterclasses are scheduled. Introduction Purinergic GPCRs, including receptors for adenosine and extracellular nucleotides, play critical roles in inflammatory signaling, neurological processes, and chronic pain biology. This session examines how structure-based approaches have guided the discovery of selective ligands targeting these receptors. Drawing on decades of medicinal chemistry research, the course explores the development of A3 adenosine receptor agonists and P2Y14 receptor antagonists, integrating chemical synthesis, pharmacological characterization, and computational modeling. Participants will also examine emerging insights into extrahelical allosteric binding sites and their implications for GPCR modulation. The session is designed for PhD scientists, postdoctoral researchers, and industry professionals interested in translational pharmacology and GPCR-targeted drug discovery. Instructors Kenneth A. Jacobson Dr. Kenneth A. Jacobson is Chief of the Molecular Recognition Section in the Laboratory of Bioorganic Chemistry at the National Institute of Diabetes and Digestive and Kidney Diseases at the National Institutes of Health. A medicinal chemist specializing in the structure and pharmacology of G protein-coupled receptors and ion channels, his research focuses particularly on purinergic receptors for adenosine, ATP, and related nucleotides. He earned a B.A. from Reed College and a Ph.D. in Chemistry from the University of California, San Diego, followed by postdoctoral training at the Weizmann Institute of Science. Dr. Jacobson’s contributions to receptor pharmacology and medicinal chemistry have been recognized with numerous honors including the Medicinal Chemistry Hall of Fame, the Smissman Award, and the Goodman and Gilman Award. His expertise underpins the strategies discussed in this Masterclass. Matteo Pavan Matteo Pavan, PhD, is a molecular modeler and visiting postdoctoral researcher in the Laboratory of Bioorganic Chemistry at the National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, working under the direction of Dr. Kenneth Jacobson. His research focuses on developing computational pipelines for rational ligand design targeting therapeutically relevant receptors, with emphasis on GPCRs within the purinergic signaling family. His work integrates molecular dynamics, virtual screening, and early-stage lead optimization to support medicinal chemistry programs. He received his PhD in Molecular Sciences from the University of Padua in 2023 under the supervision of Prof. Stefano Moro. In this Masterclass, he presents computational and SAR studies identifying an extrahelical allosteric site on the A3 adenosine receptor. Upcoming Live Sessions