Gribbon, Philip

ITMP Fraunhofer ScreeningPort Hamburg (Germany)

Curriculum Vitae: Dr Philip Gribbon

Date of Birth: 13/07/1968

Nationality : British/Irish

Contact: Fraunhofer-Institut für Translationale Medizin und Pharmakologie ITMP Schnackenburgallee 114, D-22525 Hamburg

Phone:   +49 40 303764 271



Position: Head of Discovery Research, Fraunhofer ITMP


2021 –              Head, Discovery Research, Fraunhofer ITMP, Hamburg, DE   

2014 – 2020     Co-Head of Department, Fraunhofer Institute of Molecular Biology and Applied Ecology (IME), ScreeningPort, Hamburg, DE

2008 – 2014     Chief Scientific and Operating Officer, European ScreeningPort GmbH. Hamburg, DE

2005 – 2007     Manager, GlaxoSmithKline Ltd Stevenage, UK.

2000 – 2005     Senior Principle Scientist, Pfizer Ltd, Sandwich, UK.

1995 – 1999     Post-Doctoral Research Associate, Wellcome Trust Centre for Cell-Matrix Research, University of Manchester, UK.


1991 – 1995     PhD in Biophysics, Imperial College, London.

1990 – 1991     MSc in Applied Optics, Imperial College, London.

1987- 1990      BSc (Hons) in Physics, Imperial College, London.

Other activities

2020-               Conference Chair SLAS Europe 2021, Vienna

2020-               Member European Education Committee, Society for Laboratory Automation Sciences

2019-               Chair of the Advocacy Committee, Society for Laboratory Automation Sciences

2019                Conference Chair, European Chemical Biology Symposium, Madrid

2018-2019       Chair of the Europe Committee of the Society for Laboratory Automation Sciences

2018-2020       Scientific advisor to Kaertor Foundation (Galicia, Spain)

2018-2020       Fellow of the Society of Laboratory Automation Sciences

2017                Conference Chair, European Chemical Biology Symposium, Budapest

2015-2018       Member ESFRI Life Science Infrastructure Strategy Board

2015                Conference Chair, European Chemical Biology Symposium, Berlin

2014-2018       Coordinator of EU-OPENSCREEN, the European Research Infrastructure for Chemical Biology and Screening

Selected Publications

  1. Ellinger B, Bojkova D, …Gribbon P and Ciesek S. A SARS-CoV-2 cytopathicity dataset generated by high-content screening of a large drug repurposing collection, Scientific Data 8, Article number: 70 (2021), 2021
  2. Kuzikov, M….Gribbon P and Zaliani, A. Identification of Inhibitors of SARS-CoV-2 3CL-Pro Enzymatic Activity Using a Small Molecule in Vitro Repurposing Screen, ACS Pharmacology and Translational Science 2021 (in the press)
  3. Gossen J, …Gribbon P,…Rossetti G. A Blueprint for High Affinity SARS-CoV-2 Mpro Inhibitors from Activity-Based Compound Library Screening Guided by Analysis of Protein Dynamics. ACS Pharmacology and Translational Science 2021 (in the press)
  4. Günther A…Gribbon P…and Meents A. Massive X-ray screening reveals two allosteric drug binding sites of SARS-CoV-2 main protease. (In final review) preprint here:
  5. Witt, G… Gribbon P and Pless O. An automated and high-throughput-screening compatible pluripotent stem cell-based test platform for developmental and reproductive toxicity assessment of small molecule compounds. Cell Biol Toxicol 2020.
  6. Ehrnhoefer DE, Skotte NH…Gribbon P, et al. Activation of Caspase-6 Is Promoted by a Mutant Huntingtin Fragment and Blocked by an Allosteric Inhibitor Compound. Cell chemical biology, 26 (9), 1295-1305. e6 2019
  7. Brennecke P,…Gribbon P. EU-OPENSCREEN: A novel collaborative approach to facilitate chemical biology. SLAS Discovery: Advancing Life Sciences R&d 24 (3), 398-413, 2019
  8. Sassetti E,…Gribbon P, et al. Identification and Characterization of Approved Drugs and Drug-Like Compounds as Covalent Escherichia coli ClpP Inhibitors. International journal of molecular sciences 20 (11), 2686,
  9. Moreno-Cinos C, … Gribbon P, et al. α-Amino Diphenyl Phosphonates as Novel Inhibitors of Escherichia coli ClpP Protease. Journal of medicinal chemistry 62 (2), 774-797, 2018.
  10. de Witte WEA,… Gribbon P… et al. In vitro and in silico analysis of the effects of D2 receptor antagonist target binding kinetics on the cellular response to fluctuating dopamine concentrations. British journal of pharmacology 175 (21), 4121-4136, 2018
  11. Gilardi A,…Gribbon P,… et al. Biophysical characterization of E. coli TolC interaction with the known blocker hexaamminecobalt. Biochimica et Biophysica Acta (BBA)-General Subjects, 1861 (11), 2702-2709, 2018.
  12. Korostylev A, Mahaddalkar PU, Keminer O, Hadian K, Schorpp K, Gribbon P and Lickert, H.  A high-content small molecule screen identifies novel inducers of definitive endoderm Molecular Metabolism 6(7), 640–650, 2017.
  13. De Sousa PA, … Gribbon P.. et al. Rapid establishment of the European Bank for induced Pluripotent Stem Cells (EBiSC)-the Hot Start experience. Stem cell research 20, 105-114,
  14. Borsari C….Gribbon P…et al. Profiling of Flavonol Derivatives for the Development of Antitrypanosomatidic Drugs. Journal of medicinal chemistry 59 (16), 7598-7616,
  15. Rees S, Gribbon P, Birmingham K, Janzen WP and Pairaudeau G. Towards a hit for every target. Nature Reviews Drug Discovery, 15;1–2


” Compound repurposing by target based and phenotypic approaches to identify in-vitro inhibitors of SARS-CoV2 viral entry and replication ”


Compound repurposing is an important strategy to aid the identification of effective treatment options against SARS-CoV-2 infection and COVID-19 disease. The presentation will cover the results of several repurposing programs based on phenotypic and target based screens using a large scale library of bioactive compounds. Target studies will focus on SARS-CoV-2 main protease (3CL-Pro), also termed M-Pro, which is an attractive drug target as it plays a central role in viral replication by processing the viral polyproteins pp1a and pp1ab at multiple distinct cleavage sites. We have confirmed previously reported inhibitors of 3CL-Pro and have identified 62 additional compounds with IC50 values below 1 μM and profiled their selectivity toward chymotrypsin and 3CL-Pro from the Middle East respiratory syndrome virus (see and ). In phenotypic studies, compounds were screened by microscopy for their ability to inhibit SARS-CoV-2 cytopathicity in the human epithelial colorectal adenocarcinoma cell line, Caco-2 (see These studies have been complemented by extensive structural investigations to reveal the binding characteristics of the compounds (see

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Felix Hausch

Technical University Darmstadt (Germany)

Felix Hausch is professor for structure-based drug research at the Technical University Darmstadt. He is a recognized expert for the chemical biology of immunophilins (mainly FKBPs) and has discovered the SAFit class of selective FKBP51 ligands. He has authored 82 publications (incl. Nat Chem Biol, Angew Chem, JACS; h-factor= 34 (Google Scholar)) and >10 accepted patent families. He is speaker of the LOEWE consortium TRABITA, Core team member of the Zukunftscluster PROXIDRUGS, coordinator of the BMBF consortia iMIP and 51TaValP, co-coordinator of the VIP+ consortium Fit4Fat and of the ANR/BMBF consortium SIAM. Felix Hausch received his PhD from the Free University Berlin in 2000, gained postdoc experience at Stanford University and biotech industry in Zurich (ESBATech AG, 2 years), and was group leader at the Max-Planck Institute of Psychiatry and lecturer at the LMU (Munich, 2005-2016).


De novo identification of a fully synthetic FKBP12-FRB Molecular Glue


The gain-of-function pharmacology of Molecular Glues, prominently exemplified by the immunosuppressants FK506 and Rapamycin, holds great potential to address otherwise intractable targets. So far, the known Molecular Glues have been largely discovered by serendipity or in a target-agnostic manner. To explore the probability for the existence of Molecular Glues, we performed a targeted screen for Molecular Glues for FKBP12-FRB( FKBP-Rapamycin binding domain of mTOR), using Rapamcin as an established control. From our in-house FKBP-targeted ligand library, we identified a weak hit, that was validated in an FP-based secondary assay. Surprisingly, the structure of the ternary complex revealed a new binding mode of this hit compared to Rapamycin, which allow chemical optimization resulting in a fully synthetic FBKP12-FRB Molecular Glue with sub-micromolar efficacy. Our results show that with a focused library and a tailored assay cascade a targeted de-novo screening for Molecular Glues is feasible.


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Pomplun, Sebastian

Massachusetts Institute of Technology (USA)


Combinatorial discovery of synthetic biohybrid ligands for RNA-hairpins and for the SARS-CoV-2- spike protein


The de novo discovery of ligands for challenging and novel drug targets often requires the cumbersome screening of individual compounds from large libraries. Here we present a fully chemistry based affinity selection – mass spectrometry (AS-MS) platform: within days synthetic polyamide compound libraries with > 100 million members can be produced, screened against targets of interest and originate hits with nanomolar affinity for their targets. We use AS-MS for the rapid discovery of synthetic high-affinity peptide binders for the receptor binding domain (RBD) of the SARS-CoV-2 spike protein. The peptides display excellent selectivity for RBD over human serum proteins and can detect picomolar RBD concentrations in a biological matrix. We further expanded the AS-MS platform for the discovery of compounds targeting oncogenic pre-miRNA hairpins.

In nature nucleic acids are often controlled by large supramolecular protein/oligonucleotide complexes as in the case of ribosomal protein synthesis. Rather than forming large complexes to coordinate the role of different biopolymers, we dovetail protein amino acids and nucleobases into a single low molecular weight precision polyamide polymer. We established efficient chemical synthesis and de novo sequencing procedures and prepared combinatorial libraries with up to 100 million biohybrid molecules. This biohybrid material has a higher bulk affinity to oligonucleotides than peptides composed exclusively of canonical amino acids. Using affinity selection mass spectrometry, we discovered variants with a high-affinity for pre-microRNA hairpins. Our platform points toward the development of high throughput discovery of sequence defined polymers with designer properties, such as oligonucleotide binding.

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Dal Corso, Alberto

University of Milan (Italy)

Alberto Dal Corso studied chemistry at Università degli Studi di Milano, where he obtained his Ph.D. in 2015 with Prof. Cesare Gennari. He then joined the group of Prof. Dario Neri at ETH Zürich as a postdoctoral fellow. In 2018, he returned to Università degli Studi di Milano, where he is currently working as a research fellow. In 2019 he was awarded the Junior Prize “Organic Chemistry for Life Sciences” by the Italian Chemical Society. His research interests include the development of novel drug delivery strategies and the synthesis of ligands for clinically relevant protein targets.


New-generation Self-Immolative Spacers for Fast and Controlled Release of Anticancer Drugs


Self-immolative (SI) spacers are covalent constructs capable of undergoing a spontaneous disassembly starting from a stable and inactive state, in response to specific stimuli [1]. The growing interest in the generation of stimuli-responsive devices has led to the widespread application of SI spacers in different areas, including synthetic and analytical chemistry, material sciences, and medicinal chemistry, especially in the context of prodrugs, antibody-drug conjugates, and several other drug-release strategies. We have recently described a proline-derived SI spacer that is able to release different types of anticancer drugs (possessing either a phenolic or secondary and tertiary hydroxyl groups) through a fast cyclization mechanism involving carbamate cleavage. The high efficiency of drug release obtained with this spacer was found to be beneficial for the in vitro cytotoxic activity of protease-sensitive prodrugs, compared with a commonly used spacer of the same class. Starting from these findings, novel derivatives of this proline-derived SI spacer have been designed and synthesized, either to further accelerate the drug release rates or to develop a first-in-class spacer for dual-controlled drug release. These findings expand the repertoire of degradation machineries and are instrumental for the future development of highly efficient delivery platforms.

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Cardano, Francesca

University of Milan (Italy)

Francesca Cardano is currently completing her postdoc focused on synthesis and investigations of novel chiral sensors, dyes and fluorophores for chembio applications.


Squaraine NIR dyes: a structure to function study for novel bilayer membrane probes


In the last decade, Near infra-red (NIR) fluorophores have been largely tested for bioimaging applications.[1] They typically show red-shifted absorption and emission, outstanding brightness and low photodegradation along with deep tissue penetration, small biological photodamage and negligible autofluorescence.[2] Several families of NIR dyes have been designed, synthesized
and proposed to the market for selective staining of a plethora of biological structures, but a proper modernisation in the study of cutting edge probes specific for the complex and dynamic assemblies of the bilayer membrane, is still necessary.[3] Squaraines have been already introduced to visualize and deeply study biological membranes highlighting their relevance due to singular lightness and specificity.[4] In this work, we have proposed symmetric and asymmetric squaraine dyes, decorated with carboxylic groups on the chromophoric core and different lengths aliphatic chains on the quaternary nitrogen positions of the scaffold itself. The formers facilitate the solubilization in biological media and lock the probes on the outer side of the amphiphilic bilayer, while the latter have been varied to investigate the respective interactions with the hydrophobic portion of
the membranes. The photophysical properties, the kinetic of the insertion into large unilamellar vesicles (LUVs) bilayer membranes beside with the emission signal fluctuations related to the membrane phases properties have been analysed in relation to the probe molecular structures to provide key data to optimize the design of new NIR probes for bioimaging purposes

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Marin, Riccardo

Autonomous University of Madrid (Spain)

Riccardo Marin obtained his PhD in Chemistry jointly from the University Ca’ Foscari (Venice, Italy) and the Institut National de la
Recherche Scientifique (INRS – Varénnes, Canada) under the supervision of Prof. P. Canton and Prof. F. Vetrone. He then undertook a postdoctoral fellowship at the University of Ottawa from 2017 to 2019 with Prof. E. Hemmer and Prof. M. Murugesu. He is currently a Marie Skłodowska-Curie fellow at the Universidad Autónoma de Madrid in the group of Prof. D. Jaque. His research interests encompass the development and study of optically active (nano)materials based on lanthanide ions and semiconductors.


Infrared-emitting multimodal nanostructures for controlled in vivo magnetic hyperthermia


Deliberate and local increase of the temperature within solid tumours represents an effective therapeutic approach. Thermal therapies embrace this concept leveraging the capability of some species to convert the absorbed energy into heat. To that end, magnetic hyperthermia (MHT) makes use of magnetic nanoparticles that can effectively dissipate the energy absorbed under alternating magnetic fields. Indeed, MHT is one of the very few nanoparticle-based therapeutic modalities that is currently clinical trial and that has therefore the potential to be used in the clinics. However, magnetic nanoparticles cannot provide realtime thermal feedback during MHT. As a result, unwanted overheating might occur and on-the-fly adjustment of the therapeutic parameters (such as the frequency of the alternating magnetic field) is unfeasible. Accurate, rapid, and cost-effective localization of magnetic nanoparticles within a tissue represents another challenge, which could increase the efficacy and precision of MHT. In this talk, I present the combination of iron oxide magnetic nanoparticles with state-of-the-art infrared luminescent nanothermometers (Ag2S nanoparticles) in a nanocapsule that simultaneously overcomes these limitations. The novel optomagnetic nanocapsule acts as multimodal contrast agent for different imaging techniques (magnetic resonance, photoacoustic, infrared fluorescence, optical tomography, and X-ray computed tomography). Most crucially, this nanocapsule
provides accurate (0.2 ⁰C resolution) and real-time subcutaneous thermal feedback during in vivo MHT, also enabling the attainment of thermal maps of the area of interest. These findings are a milestone on the road towards controlled magnetothermal therapies with minimal side effects.

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Pizzolitto, Chiara

University of Trieste ( Italy)

Chiara Pizzolitto received master’s degree in nanobiotechnology in 2019. Currently she is a second year PhD student at University of Trieste.


Dual cross-link hydrogels with tunable viscoelasticity control stem cell differentiation


Mechanotransduction recapitulates the conversion of external mechanical information into intracellular biochemical response. To this, it was recently recognized that stem cell fate can be markedly influenced by surrounding extracellular matrix (ECM) mechanics. Most of our knowledge in cell mechanobiology has been built using purely elastic materials as model of ECM. However, native tissues do not exhibit purely elastic response but manifest viscoelasticity, that is a time- and frequencydependence to loading. In fact, recent works have proved that stress-relaxation or plasticity, and more broadly, viscosity-driven processes can be considered as potent modulators of stem cell behavior. To recapitulate native tissue mechanics and provide a more realistic ECM model, here we present unprecedented viscoelastic substrates showing adaptable viscoelasticity. In particular, I will present an innovative dual cross-link gel system based on a chitosan derivative, shortly named CTL, assembled via both temporary and permanent cross-linkers.[1] Concepts related to macromolecular chemistry and physics will be disclosed. Of note, temporary junctions are exploited to finely tune material viscoelasticity. I will show how resulting hydrogels result optimal substrates for cell anchoring upon coating with ECM proteins. Though endowed with similar elasticity, a viscositycell function relationship will be unveiled, identifying high viscosity hydrogels as superior materials in fostering stem cell differentiation toward a bone-like phenotype with respect to more elastic counterparts. Taken together, these results lay the groundwork for additional investigations on the role played by substrate viscoelasticity in directing cell-fate decisions.

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Astolfi, Andrea

University of Perugia (Italy)


A novel class of small molecule degraders targeting prion protein folding intermediate


Decades of research efforts have conclusively provided overwhelming evidence that the cellular prion protein (PrPC) represents an optimal pharmaceutical target to tackle prion diseases, a set of fatal and incurable neurodegenerative disorders characterized by the conformational conversion of the physiological PrPC into a misfolded and infectious isoform referred to as PrP scrapie (PrPSc). Indeed, PrPC plays a key role in the disease etiology and knock-out experiments demonstrated that its therapeutic suppression can be considered safe. Over the years different strategies have been proposed to tackle this target based on traditional drug discovery approaches, such as the identification of small molecules able to promote the PrPC relocalization from cellular membrane to intracellular endosomes, as well as PrPC binders that prevent its conversion to PrPSc. However no therapy is yet available, and prion disease still represents a currently unmet medical need. Very recently, we have applied a novel drug discovery approach devoted to lowering PrPC levels by hampering a complete folding process. We refer to this strategy as Pharmacological Protein Inactivation by Folding Intermediate Targeting (PPI-FIT). The reconstruction of the PrP folding pathway through all-atoms MD simulation allowed the identification of a metastable intermediate of the PrP folding pathway characterized by a druggable pocket. Virtual screening of a commercial small molecule library resulted in the identification of thirteen potential binders, four of which capable of selectively lowering the load of PrP into the cellular membrane and promote its degradation. Additionally, one of these compounds inhibits prion replication in a dose-dependent fashion.

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Antolin, Albert

The Institute of Cancer Research, London (United Kingdom)

Dr. Albert Antolin obtained a PhD in Pharmacoinformatics (Pompeu Fabra University,Spain) pioneering the application of polypharmacology prediction to chemical biology by uncovering off-targets of chemical probes. Dr. Antolin was subsequently awarded a Marie Curie Fellowship to join the Institute of Cancer Research (UK) to develop the first objective resource for the assessment of chemical probes ( Next, Dr. Antolin won a Wellcome Fellowship to explore the polypharmacology of cancer drugs and their implications for precision oncology. Having worked in industry and academia, Dr. Antolin is interested in bridging industrial drug discovery with remaining fundamental questions in cancer chemical systems biology


From probe to drug: Polypharmacology across drug discovery


Most small molecules interact with several target proteins but this polypharmacology is seldom comprehensively investigated or explicitly exploited during drug discovery. Here, we present the use of computational and experimental methods to identify and systematically characterize the kinase cross-pharmacology of representative HSP90 and PARP inhibitors. We demonstrate that the HSP90 inhibitors ganetespib and luminespib and the PARP inhibitors rucaparib and niraparib display unique off-target kinase pharmacology as compared to other clinical inhibitors of the same class, with important implications for personalized prescription. We also demonstrate that the early PARP chemical tool PJ34 displays a different polypharmacology than several FDA-approved PARP inhibitors, with important implications for target validation and the practise of chemical biology. We finally demonstrate that polypharmacology evolved during the optimisation to discover luminespib and that the hit, leads and clinical candidate all have different polypharmacological profiles. We therefore recommend the computational and experimental characterization of polypharmacology earlier in drug discovery projects to unlock new multi-target drug design opportunities as well as identifying undesired toxicity and unexplained cellular effects.

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Matamoros-Recio, Alejandra

Center for Biological Research Margarita Salas (Spain)

Alejandra Matamoros-Recio received a postgraduate from the University of Alcalá, Madrid (M.Sc. in Drug Discovery 2017). She is a predoctoral research fellow in the “Computational Biological Chemistry” group led by Dr. Sonsoles Mart́ın-Santamaría, at CIB Margarita Salas, CSIC (Spain), pursuing a Ph.D. at the University Complutense of Madrid. Her research project lies at the interface between Chemistry and Biology, by means of molecular modeling and computational chemistry, applied to the understanding of ligand-receptor interactions and molecular recognition processes relevant for drug design, with a particular focus on Toll-like receptors and Antimicrobial Resistance-related receptors


Computational approaches to the dynamics and activation mechanism of Toll-like receptor 4


Toll-like receptors (TLRs) are pattern recognition receptors involved in innate immunity. In particular, TLR4 binds to lipopolysaccharides (LPS), a membrane constituent of Gram-negative bacteria and, together with MD-2 protein, forms a heterodimeric complex which leads to the activation of the innate immune system response. TLR4 activation has been associated with certain autoimmune diseases, noninfectious inflammatory disorders, and neuropathic pain, suggesting a wide range of possible clinical settings for the application of TLR4 antagonists, while TLR4 agonists would be useful as adjuvants in vaccine development and in cancer immunotherapy. Specific molecular features of extracellular, transmembrane, and cytoplasmic domains of TLR4 are crucial for coordinating the complex innate immune signaling pathway. Although structural and biochemical data is currently available for the independent TLR4 domains, this only provides a partial fragmented view, because full-length proteins are flexible entities and dynamics play a key role in their functionality. Therefore, many structural and dynamical features of the TLR4 mode of action remain largely unknown. Computational studies of the different independent domains composing the TLR4 were undertaken, using ab-initio calculations, homology modeling, protein-protein docking, all-atom molecular dynamics simulations, and thermodynamics calculations, to understand the differential domain organization of TLR4. From the information gathered from our independent TLR4 domains studies, we have modeled, by allatom MD simulations, the structural assembly of plausible full-length TLR4 models embedded into realistic plasma membranes, with different chemical compositions, accounting for the active (agonist) state of the TLR4. We have also applied computational techniques to characterize, at the atomic level, the molecular recognition processes by reported TLR4 modulators, thus proposing a mechanism for their biological activity. These observations unveil relevant molecular aspects involved in the mechanism of receptor activation, and adaptor recruitment in the innate immune pathways, and will promote the discovery of new TLR4 modulators and probes.

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