What drives us at CELLinib is the thought to speed up your drug discovery project using our expertise in small molecule profiling in living cells using the NanoBRET^TM technique – and that you may reach your project goal faster by considering your small molecule’s effect in living cells!

We want to speed up your drug discovery project by quickly and accurately characterizing your small molecule inhibitor across the kinome in living cells using the Promega NanoBRET^TM technology. Let’s illuminate science together!

Our History

Both of us are SGC scientists and love to collaborate with many different scientists around the world on all their fantastic projects – we even established the NanoBRET^TM technique as a standard for the characterization of kinase small molecules within the donated chemical probe project of the SGC with many pharma partners. We often contributed NanoBRET^TM profiling data to help explore an inhibitor mechanism, discover inhibitor target engagement in living cells, do an off-target profiling or conduct large mutagagenesis studies. We have become experts in delivering accurate data very quickly – with established workflows and quality controls. Now, we just love to use NanoBRET^TM as a method to quickly and accurately get quality data to answer our biological questions.

We have been trained by the two best experts in the field: Prof. Dr. Stefan Knapp is the expert on protein kinase structure and inhibitor development. Dr. Susanne Müller-Knapp is the expert for small molecule selectivity of chemical probes and manages the donated chemical probes program and the chemical probes portal. Hence, it was clear we would set out to develop a comprehensive platform for cellular selectivity characterization of protein kinase inhibitors – so we created this representative profiling and serveral services around this in living cells.

Within the SGC Frankfurt we helped to develop chemical probes – highly characterized chemical molecules that will be able to answer biological questions – e.g. determining a target in a phenotypic screen. Because these molecules are later tested in living cells it is absolutely crucial to know their target engagement profile in living cells! We delivered this data and helped to determine the concentration at which it is safe to use the probe without off-target interference – but still at a reasonable concentration to observe the on-target effect!

We also both have industry experience with inhibitor characterization where we had the honour to work as students at Bayer HealthCare (Berlin) and Merck KGaA (Darmstadt). We now want to work together with you to make sure your inhibitor engages its designed target in living cells.

Our Promise

We will profile your small molecule inhibitor with accuracy, speed and dedication.

Our recent projects

Please browse through the amazing projects we were allowed to contribute to. Thanks for the trust from all our collaborators!

Projects about the NanoBRET^TM technique

Robers et al. (STAR Protoc., 2021): Single tracer-based protocol for broad-spectrum kinase profiling in live cells with NanoBRET.
– a protocol on how to perform a screen of 192 protein kinases in NanoBRET

Robers et al. (Annu Rev Biochem., 2020): Quantifying Target Occupancy of Small Molecules Within Living Cells.
– a great review about target engagement methods

Vasta et al. (Cell Chem Biol., 2018): Quantitative, wide-spectrum kinase profiling in live cells for assessing the effect of cellular ATP on target engagement.
– cellular profiling is crutial and differs from in vitro profiling

Projects focusing on cellular profiling

Bata et al. (J Med Chem., 2022): Inhibitors of the Hippo Pathway Kinases STK3/MST2 and STK4/MST1 Have Utility for the Treatment of Acute Myeloid Leukemia.
– cellular characterization that lead to a selective probe for STK3 and STK4

Röhm et al. (J Med Chem., 2021): Development of a Selective Dual Discoidin Domain Receptor (DDR)/p38 Kinase Chemical Probe.
– cellular characterization that lead to a probe for p38 and DDR1/2

Russ et al. (J Med Chem., 2021): Design and Development of a Chemical Probe for Pseudokinase Ca2+/calmodulin-Dependent Ser/Thr Kinase.
– cellular characterization for the pseudokinase CASK

Wittlinger et al. (J Med Chem., 2021): Design of a “Two-in-One” Mutant-Selective Epidermal Growth Factor Receptor Inhibitor That Spans the Orthosteric and Allosteric Sites.
– cellular characterization for EGFR

Tesch et al. (J Med Chem., 2021): Structure-Based Design of Selective Salt-Inducible Kinase Inhibitors.
– cellular characterization of inhibitors for the (hard to express) SIK family

Reynders et al. (Angew Chem Int Ed Engl., 2021): Controlling the Covalent Reactivity of a Kinase Inhibitor with Light.
– cellular characterization of a light-inducible JNK1 inhibitor

Krishnathas et al. (FASEB J., 2021): C81-evoked inhibition of the TNFR1-NFκB pathway during inflammatory processes for stabilization of the impaired vascular endothelial barrier for leukocytes
– off-target profiling of natural compound C81 on various protein kinases

Němec et al. (Eur J Med Chem., 2021): Highly selective inhibitors of protein kinases CLK and HIPK with the furo [3, 2-b] pyridine core.
– cellular characterization of inhibitors for the CLK and HIPK family

Mathea et al. (Biochem J., 2021): Conformational plasticity of the ULK3 kinase domain.
– cellular characterization of inhibitors for ULK3

Krämer et al. (Eur J Med Chem., 2020): Optimization of pyrazolo[1,5-a]pyrimidines lead to the identification of a highly selective casein kinase 2 inhibitor.
– cellular characterization of CK2 inhibitors – in particular a macrocyclic inhibitor

Röhm et al. (Eur J Med Chem., 2020): Selective targeting of the αC and DFG-out pocket in p38 MAPK.
– cellular characterization of p38 inhibitors

Pedreira et al. (J Med Chem., 2020): Bioisosteric Replacement of Arylamide-Linked Spine Residues with N-Acylhydrazones and Selenophenes as a Design Strategy to Novel Dibenzosuberone Derivatives as Type I 1/2 p38α MAP Kinase Inhibitors.
– cellular characterization of p38 inhibitors

Hanke et al. (ACS Chem Biol., 2020): A Highly Selective Chemical Probe for Activin Receptor-like Kinases ALK4 and ALK5.
– cellular profiling among the ALK family

Röhm et al. (J Med Chem., 2019): A fast iterative synthetic approach towards the identification of novel highly selective p38 MAP kinase inhibitors.
– cellular characterization of p38 inhibitors

Němec et al. (Angew Chem Int Ed Engl., 2019): Furo [3, 2‐b] pyridine: A Privileged Scaffold for Highly Selective Kinase Inhibitors and Effective Modulators of the Hedgehog Pathway.
– cellular characteriztaion lead to highly specific CLK inhibitors

Asquith et al. (J Med Chem., 2019): SGC-GAK-1. A chemical probe for cyclin G associated kinase.
– cellular profiling revealed that our GAK probe is in fact a dual GAK/RIPK2 probe

Tröster et al. (ChemMedChem., 2018): NVP‐BHG712: Effects of Regioisomers on the Affinity and Selectivity toward the EPHrin Family.
– inhibitor profiling among the Ephrin family

Forster et al. (J Med Chem., 2018): Development, optimization, and structure–activity relationships of covalent-reversible JAK3 inhibitors based on a tricyclic imidazo [5, 4-d] pyrrolo [2, 3-b] pyridine scaffold.
– inhibitor profiling in living cells on JAK3

Projects about mutagenesis studies and cellular half-lives using NanoBRET^TM

Lyczek et al. (Proc Natl Acad Sci U S A., 2021): Mutation in Abl kinase with altered drug binding kinetics indicates a novel mechanism of imatinib resistance.
– large mutagenesis study to identify fast cellular half-lives as a mechanism for imatinib resistance

Berger et al. (Cell Chem Biol., 2021): Structure-kinetic relationship reveals the mechanism of selectivity of FAK inhibitors over PYK2.
– study on cellular half-lives of FAK/PYK2 inhibitors deciphering their mechanism via a mutagenesis study

Projects on the cellular characterization beyond protein kinases

Dölle et al. (J Med Chem., 2021): Design, Synthesis, and Evaluation of WD-Repeat-Containing Protein 5 (WDR5) Degraders.
– it does not always have to be kinases – here we profiled inhibitors for WDR5 in cells

Zhang et al. (Int J Cancer., 2020): Characterization of a dual BET/HDAC inhibitor for treatment of pancreatic ductal adenocarcinoma.
– it does not always have to be kinases – here we profiled dual inhibitors for BRD4 and HDAC1 in cells