Shining Light on Innovation:
A Day to Explore Luminescent Technologies and Automation
Innovation Day 2024 - Explore Luminescent Technologies and Automation
Join us for a day of scientific discussions along with experts from Academic, Pharmaceutical and Biotechnology companies.
We're pleased to announce that Promega Benelux is hosting two Innovation Days this May, taking place in Amsterdam and Leuven.
These gatherings are a unique opportunity to delve into the latest scientific advancements, presented by both our Promega scientists and distinguished guests from academia, pharmaceuticals, and biotechnology sectors.
This will be a chance to engage in meaningful discussions, broaden your knowledge, and connect with experts and peers in an informal setting.
There is no charge for attendance – breaks and lunch are on us. But we like you to sign up so we secure your seat and prepare some healthy food and beverages.
Whether you have a deep interest in science or are looking to catch up with the latest trends and innovations, these days are designed for you. It's an ideal moment for networking, learning, and sharing experiences in a relaxed yet stimulating environment. We're looking forward to welcoming you to what we hope will be insightful and rewarding days of scientific exploration and collaboration.
Dates and Locations
Amsterdam : Tuesday 28 May 2024
Our venue in Amsterdam is the inspirational O|2 Building on the VU-campus.
De Boelelaan 1108
1081 HZ Amsterdam
Leuven : Wednesday 29 May 2024
Our venue in Leuven is the well-known knowledge hub ON4 at Gasthuisberg Campus.
KU LEUVEN
ON4 Herestraat 49
3000 Leuven
Building: 404-24
Agenda and Registration
Amsterdam - Tuesday 28 May
| Time | Talk |
|---|---|
| 09:00 | Arrival, Registration and Coffee |
| 09:30 | Welcome & opening remarks Lindsay Mesure, Product Specialist & Sales Manager Promega BNL |
| 09:40 |
Antibody format induced receptor co-localization: to BRET or to FRET that is the question |
| 10:15 | Target engagement cooperativity at intracellular complexes for synthetic lethal drugs Matt Robers Promega Corporation, USA Read Abstract | View Bio |
| 10:50 | Coffee Break |
| 11:10 | Biosensing Molecular G Protein-Coupled Receptor (GPCR) Pharmacology Dr. Henry Vischer Assistant Professor of Molecular Pharmacology at the Vrije Universiteit Amsterdam, The Netherlands Read Abstract | View Bio |
| 11:45 |
From vision to viability: unveiling the future with GloMax Galaxy bioluminescence imager and MyGlo cell health reader |
| 12:30 | Complimentary Lunch and Poster Session |
| 13:00 | Optional session: Optimizing efficiency: showcasing Maxwell extraction instrument with a special focus on exosome and miRNA isolation & high-throughput automation
Dr. Henk Honing Technical Operations and Partnerships Manager, Promega BNL Read Abstract | View Bio |
| 13:30 | Targeted protein degradation of GPCRs: a novel approach to target CCR2 Dr. Natalia Ortiz Zacarías Postdoctoral Researcher, Molecular Pharmacology at the Leiden Academic Centre for Drug Research (LACDR), Leiden, The Netherlands Read Abstract | View Bio |
| 14:05 | Developing robust, quantitative assays on a high-throughput organ-on-chip platform Flavio Bonanini Early Stage Researcher, MIMETAS, Oegstgeest, The Netherlands Read Abstract | View Bio |
| 14:40 | Newest assay developments highlights – Innovation never stops Dr. Lindsay Mesure Product Specialist & Sales Manager Promega Benelux Read Abstract | View Bio |
| 15:15 | Closing Remarks and Refreshments |
Leuven - Wednesday 29 May
| Time | Talk |
|---|---|
| 09:00 | Arrival, Registration and Coffee |
| 09:30 | Welcome & opening remarks Lindsay Mesure, Product Specialist & Sales Manager Promega BNL |
| 09:40 |
Nanoclick as potential tool to assess receptor mediated internalization |
| 10:15 | Target engagement cooperativity at intracellular complexes for synthetic lethal drugs Matt Robers Promega Corporation, USA Read Abstract | View Bio |
| 10:50 | Coffee Break |
| 11:10 | Systematic assessment of chemokine ligand bias at the human chemokine receptor CXCR2 indicates G protein bias over β-arrestin recruitment and receptor internalization Katrijn Boon Ph.D. student; Laboratory of Virology and Chemotherapy, Rega Institute for Medical Research, Leuven, Belgium Read Abstract | View Bio |
| 11:45 |
From vision to viability: unveiling the future with GloMax Galaxy bioluminescence imager and MyGlo cell health reader |
| 12:30 | Complimentary Lunch and Poster Session |
| 13:00 | Optional session: Optimizing efficiency: showcasing Maxwell extraction instrument with a special focus on exosome and miRNA isolation & high-throughput automation
Dr. Henk Honing Technical Operations and Partnerships Manager, Promega BNL Read Abstract | View Bio |
| 13:30 | Illuminating the small proteome of Salmonella
Laure Simoens Ph.D. student at the Department of Biochemistry and Microbiology, Ghent University, Ghent, Belgium Read Abstract | View Bio |
| 14:05 | Activity-based detection of drugs and performance enhancing substances: the versatility of various NanoBiT assays
Liesl Janssens Ph.D. student at the Department of Bio-Analysis, Ghent University, Ghent, Belgium Read Abstract | View Bio |
| 14:40 | Newest assay developments highlights – Innovation never stops Dr. Lindsay Mesure, Product Specialist & Sales Manager Promega Benelux Read Abstract | View Bio |
| 15:15 | Closing Remarks and Refreshments |
Speakers and Abstracts
Promega Speakers
Matt Robers, Promega Corp., USA
In cancer, loss of function mutations expose collateral vulnerabilities and opportunities for precision medicines. Genetic lesions in DNA repair or metabolic machinery can result in the accumulation of intracellular byproducts that form inhibitory biomolecular protein complexes. Stabilization of such complexes can result in a selective loss of cancer cell fitness. The PRMT5 methyltransferase has a global role in cell physiology its activity is tightly regulated by the intracellular pool of metabolic derivatives of S-adenosylmethionine (SAM). Described small molecule PRMT5 inhibitors engage either SAM- or peptide-substrate pockets through diverse mechanisms. A subset of chemotypes demonstrate cooperativity with SAM and its inhibitory metabolic precursor, MTA. In >10% of human cancers, deletion of the MTAP gene results in accumulation of MTA supporting a synthetic lethality and opportunity for precision medicine at PRMT5. We’ve new NanoBRET methods to mechanistically characterize and quantify ternary complex formation at synthetic lethal protein complexes in cancer cells. Using PRMT5 and polymerase theta as prototypes, this new method can be used to quantify uncompetitive target engagement at protein complexes as generalizable tool for synthetic lethal drug screening.
Lindsay Mesure, Promega Benelux
Henk Honing, Promega Benelux
Guest Speakers Amsterdam
Els van der Meijden, Genmab
Flavio Bonanini, MIMETAS
I grew up in Southern Switzerland and relocated to Zurich in 2012 to commence my undergraduate studies in Biology at the Swiss Federal Institute of Technology (ETH). Subsequently, I pursued a Master's degree in Biomedical Engineering, with a specialization in tissue engineering, also at ETH, and successfully completed my studies in 2018.
From 2019, I have been a Marie Sklodowska-Curie fellow student affiliated with MIMETAS, a biotech company located in Leiden, Netherlands, as part of the PoLiMeR consortium. In my current role, I focus on liver models and contribute to the development of a throughput-capable organ-on-chip culture platform, which MIMETAS specializes in developing and commercializing.
Henry Vischer, VU Amsterdam
Natalia Ortiz Zacarías, LACDR
Natalia Ortiz Zacarías completed her PhD in the field of Medicinal Chemistry at the Leiden Academic Centre for Drug Research (LACDR), Leiden University. Her PhD thesis was awarded the 2019-2020 best thesis prize from the KNCV-Medicinal Chemistry & Chemical Biology (MCCB). After her PhD, she continued working as a Postdoctoral Researcher at both the LACDR and Oncode Institute, focusing on novel pharmacological concepts to better target chemokine receptors in cancer. In 2021, she worked as Research Scientist in the startup ARTICA Therapeutics, focusing on the characterization of novel small-molecule drugs. In 2021 she also obtained a Veni grant from the Dutch Research Council (NWO) for her project “Towards illuminating and modulating chemokine receptor fate”, which she is currently performing at the group of Prof. Heitman, at the LACDR and Oncode Institute.
Guest Speakers Leuven
Katrijn Boon, Rega Institute
Laure Simoens, Ghent University
By bridging transcriptomics and translatomics information, ribosome profiling by sequencing (Ribo-seq) has been a game-changer for bacterial genome (re)annotation, this way feeding the pool of information on putative, protein-coding regions. Especially for the genomic discovery of small open reading frames (sORFs), which maximally comprise 300 base pairs (bp) and therefore were for a long time considered as noise by standard annotation algorithms, Ribo-seq has proven indispensable. Despite their clear involvement in basic bacterial functioning and even in bacterial infection, the protein products of this specific class of genomic elements, the sORF-encoded polypeptides (SEPs), are particularly understudied because of their small sizes (i.e. maximal protein length of 100 amino acids (AA)) and also their relatively higher hydrophobicity and presumed unstable nature, together hindering detection by standard protein detection methods. As a result of the limited number of tryptic peptides from SEPs and the overall lower detectability of the (often) hydrophobic peptides, mass spectrometry-based detection of SEPs is difficult and sometimes even impossible, making the proteome-wide expression validation of bacterial Ribo-seq-inferred putative SEPs a difficult task.
To complement mass spectrometry-based validation of bacterial SEP expression, we focus on the development of a toolkit for efficient and endogenous small protein detection in Salmonella Typhimurium relying on the NanoLuc Binary Technology (NanoBiT, Promega) which allows for highly sensitive as well as highly specific, luminescence-based detection of proteins tagged with the very small (11 AA) peptide tag HiBiT. NanoBit is based on the reconstitution of an active luciferase upon the interaction between the HiBiT tag and its complementing protein LgBiT and can be used for the detection of HiBiT-tagged proteins both through blotting (i.e. HiBiT blotting) and in solution detection (i.e. lytic HiBiT detection). In addition to SEP expression in general, the detection tool can be implemented for the study of SEP secretion, subcellular localization, stability, and expression dynamics, which can help to understand their physiological relevance. Based on this information, interesting Salmonella SEP candidates are filtered out for more functional investigation through interactomics (proximity-based biotin identification, BioID) and phenomics (phenotype microarrays, PM).
As an enormous part of the bacterial small proteome is still unexplored, a whole piece of knowledge on bacterial biology might be missing. Using our comprehensive, NanoBiT-centered workflow; integrating annotation, experimental expression validation, subcellular localization determination, and interactome characterization; in the bacterial model organism Salmonella Typhimurium, we will participate in the broadening of general knowledge on bacterial SEP biology and in expanding the technical toolkit facilitating small protein biology discoveries.
Liesl Janssens, Ghent University
Over the past years, several NanoBiT® Technology-based bioassays have been developed at the Laboratory of Toxicology of Ghent University, to allow activity-based detection and characterization of drugs in live cells. Cellular proteins of interest have been molecularly coupled to SmallBiT and LargeBiT and stably introduced into human embryonic kidney (HEK293T) cells to monitor the bioactivity manifested by drugs (e.g., cannabinoid, opioid or serotonin receptor activation). The luminescent readout of these bioassays serves as a measure of biological activity, which has been interpreted for various applications. Similar to other functional assay systems, these bioassays have allowed pharmacological characterization and toxicological investigation of compounds, including the assesment of structure-activity relationships, with applications in medicinal chemistry. Importantly, these bioassays are used by the Laboratory of Toxicology as universal screening tools to detect the presence of abused compounds in human biofluids (e.g., blood, serum, plasma, urine, saliva). Activity-based detection of drugs has the intrinsic advantage of eliminating the need for prior knowledge of the chemical fingerprint in order to detect drugs. Furthermore, every drug with bioactivity is detected by the system, regardless of the chemical structure. This untargeted detection approach is particularly of interest for the detection of designer drugs – which are drugs that are chemically designed or altered in clandestine laboratories to evade detection.
Most recently, new bioassays were developed for the detection of doping substances. These bioassays were designed to serve as an activity-based screening tool for the detection of doping in athlete urine samples. Doping control currently relies on mass spectrometry-based detection methods for the screening of athlete samples for a long list of possible performance enhancing substances. This targeted detection approach is challenged by the emergence of designer drugs and ample clinical candidate molecules that are being researched for therapeutic use. Moreover, “you won’t find what you’re not looking for”. Every compound that is not included in the targeted testing procedure will be missed. This is in contrast with the unlimited ban by the World Anti-Doping Agency that prohibits the use of all drugs with performance enhancing effects. By refocussing the detection mechanism to detect biological activity one could say that “you can find what you’re not (specifically) looking for”. Every compound that is bioactive will be picked up by activity-based testing. Hence, these new bioassays are meant as future-proof screening tools, capable of detecting known and unknown/emerging substances.
In this presentation, I will present the development of a new doping bioassay, capable of detecting activitity of so-called HIF (hypoxia-inducible factor) stabilizers. Moreover, the versatility of the generated NanoBiT® assays will be demonstrated. Several innovative applications will be highlighted, covering different interpretations of the biological readout. In addition, potential optimization opportunities will be discussed for the design of bioassays that have allowed our cell-based assays to be used for the investigation of human biofluids.
I started my academic studies at Ghent University in 2014 with a Bachelor in Pharmaceutical Sciences. Growing an interest in scientific research, I deliberately continued with a Master in Drug Development to broaden my view on Research & Development. This is where I fell head over heels for the endless possibilities of biotechnology leading to innovation.
Hence, I started my PhD in the laboratory of Toxicology of Prof. Christophe Stove, developing new cell-based assays as a future-proof testing strategy for doping substances. Working in the laboratory of Toxicology, naturally brought me into contact with drug research, leading to a common thread: activity-based detection to cope with the emergence of designer drugs. I continued my PhD, dividing my attention between my main research line on doping and ongoing research in the laboratory on synthetic drugs. Almost 5 years later, I am ready to submit my PhD on the untargeted detection of performance-enhancing drugs and the versatility of cell-based assays.
Viviana Gatta, UCB BioPharma
Cytosolic bioavailability is a strong limiting factor for the development and delivery of new therapeutics active intracellularly. In fact, the majority of molecules gets internalized and redirected to lysosomes for degradation. Determining endosomal escape and cytosolic presence of potential drug candidates at early stage of the screening cascade can significantly impact the drug discovery process. To answer this need, Nanoclick has been described as high-throughput and target agnostic assay which combines click chemistry and Nano-Bret signal for the detection of cell-penetrating peptides. We explored the potential of the assay to assess internalization of molecules mediated by specific protein of interest. We will describe the optimization of live and digitonin conditions to enable determination of endosomal escape as well as the development of a target deficient line to confirm molecules specificity. This flexible setup can be adapted to different kind of therapeutics and targets, enabling the use of Nanoclick as tool for the discovery of target-mediated internalization.
Viviana Gatta1, Noemie Willain2, Davide Proverbio2, Martine Geraerts1
1 UCB BIOPHARMA SRL, In Vitro Pharmacology Research, Avenue de l’ Industrie 1420 Braine l’Alleud
2 NOVALIX SAS, 16 rue d'Ankara, 67000 Strasbourg, France
Viviana joined UCB (Belgium) in 2019 as scientist specialized in assay development and screening to support pre-clinical CNS projects. With several years of experience in in vitro activities, she brings a wide set of expertise in drug discovery to her role. She holds a Ph.D. in Drug Discovery from the University of Helsinki, where her research focused on implementing biochemical and cell-based assays for the discovery of novel antimicrobial agents. Her doctoral work, funded by the prestigious Horizon 2020 program, exemplifies her commitment to cutting-edge research and innovation in the field.
