Stephanie Anbuhl wins poster prize on the annual MCCB KNCV meeting in Lunteren

On Thursday the 30th of March 2023, our talented early-stage researcher (ESR) within the ITN project ONCORNET2.0, Stephanie Mareike Anbuhl , presented her poster on the reformatting of improved CXCR4-targeting single domain antibodies for biophysical detection methods on the annual meeting of the Medicinal Chemistry & Chemical Biology (MCCB) division of the Royal Netherlands Chemical Society (KNCV) in Lunteren. On her poster, Stephanie illustrated how various immunization and phage display approaches can aid the development of novel CXCR4 binding single domain antibodies against previously untargeted epitopes or conformations and with unprecedented affinity and potency. Also, Stephanie showed examples how such molecules can be developed into higher order multivalent formats for improving potencies even further as well as conjugating them to make … Read more

NanoB2 for assessing binding of ligands to drug targets

In a collaborative project, researchers at QVQ (Stephanie Mareike Anbuhl and Raimond Heukers), VU Amsterdam (Martine Smit lab) and University of Nottingham (Laura Kilpatrick and Steve Hill) have developed a novel approach using labeled VHH to easily assess and quantify binding of ligands to different drug targets. This technology, named NanoB2 (nanobody-NanoBRET), was published in the journal of Cell Reports Methods. The work, driven by Jelle van den Bor and Nick Bergkamp proves again the high potential of labeled VHH as detection agents. In this new technology, labeled VHH are used for the determination of the binding sites, kinetics and affinities of unlabeled drugs and thereby aid the identification of novel ligands.  Link

Fluorescently tagged nanobodies

QVQ recently contributed to a study that nicely exemplifies directionally fluorescently labelled single domain antibodies as extracellular receptor conformation sensors. This is a result of a smooth ONCORNET2.0 collaboration, in this case led by Laura Kilpatrick and Steve Hill. Link

Candidalysin causes C. albicans-associated haemolysis

Candida albicans is an opportunistic yeast naturally occurring on our body. This yeast can become pathogenic causing candidiasis. Candidalysin, a peptide toxin secreted by the fungus, is involved in Candida becoming pathogenic the  mediates its translocation through intestinal epithelium causing serious infections. A recent study led by prof. Bernard Hube now shows that Candidalysin is also the driver of C. albicans-associated haemolysis. This process can be fully inhibited by two single domain antibodies. Link