We show that peptides mimicking the CDR3 of a Nanobody can modulate protein-protein interactions 

Jan Steyaert is the 24th (2022) winner of the Jacob and Louise Gabbay Award in Biotechnology and Medicine in recognition of his contributions to structural biology through the development of Camelid single-domain antibodies or nanobodies

Nanobodies developed in our lab were instrumental to solve different structures of the human NTCP, revealing key conformations of its transport cycle. NTCP is the main bile salt uptake system in liver and is the cellular entry receptor of human hepatitis B and D viruses.

Different cryo-EM structures of the hyaluronan synthase provide insights into the biosynthesis of one of the most abundant and essential glycosaminoglycans in the human body

As Nanobodies were born at the University of Brussels, the VIB-VUB Center for Structural Biology was very honored to organize the hybrid second edition of bianual Nanobody conferences.

New nanobody-based tools to improve structure determination by single-particle cryo-EM

According to Dimensions data, they have co-authored 101 papers together since 2009, 45 of which were published in journals tracked by the Nature Index. They also hold 93 patents related to their nanobodies technique.

We reported several high-resolution cryo-electron microscopy structures of the human heterotrimeric GABAA receptor bound to several ligands including alprazolam and diazepam.

By fusing Nanobodies that exhibit G protein-like behavior, we were able to lock GPCRs constitutively in their active conformation. These GPCR-Nb fusions have a unique pharmacological profile.

Confo Therapeutics’ unparalleled technology stabilizes functional conformations of GPCRs (G protein-coupled receptors) to uncover a wide range of previously inaccessible GPCRs as drug targets.

Nanobodies from our lab were instrumental to lock and solve the structures of inward-facing conformations of P-glycoprotein, LacY, an Fe2+ transporter, a fumarate transporter and the mitochondrial ADP-ATP transporter.

In collaboration with several groups, we started applying our Nbs as versatile tools for the investigation of GPCR dynamics at the molecular and the sub-cellular level in vitro or as intrabodies inside cells.

In collaboration with the Kobilka lab we generated Nb35 that freezes a transient Adrenergic Receptor-Gs protein complex

In collaboration with Brian Kobilka, In collaboration with Brian Kobilka, we generated Nanobodies against the β2 adrenergic receptor (β2AR), the muscarinic acetylcholine receptor (M2R) and the μ-opioid receptor (MOR) that exhibit G protein-like behaviour, and obtained agonist-bound, active-state crystal structures of receptor●Nb complexes of β2AR, M2R & MOR.