At IRBM, we are passionate about understanding the underlying biology of disease, to drive drugdiscovery. In a recent paper funded by our consortium partner CNCCS, we evaluated the efficacy of a PEGylated Ciliary Neurotrophic Factor (CNTF) super-agonist variant in diet-induced obese mice.
IRBM & Heidelberg University Hospital publishes in Cell Reports Medicine on kynurenine pathway activation and deviation to anthranilic and kynurenic acid in fibrosing chronic Graft-Versus-Host Disease
Our Biomarkers team, in collaboration with Dr. Thomas Luft group at the Heidelberg University Hospital (Germany), explored the role of…
Guiding chemically synthesized peptide drug lead optimization by de-risking mast cell degranulation related toxicities of a NaV1.7 peptide inhibitor
Peptides can induce non IgE-mediated anaphylactoid reactions. These effects are triggered by the direct interaction of the peptide with mast cells that result in their degranulation and release of histamine and other inflammatory mediators.
Development of ProTx-II Analogues as Highly Selective Peptide Blockers of Nav1.7 for the Treatment of Pain
Targeting ion channels involved in nociception is currently being investigated for the treatment of pain. Human genetic studies have demonstrated that patients with null mutations in the voltage-gated sodium channel Nav1.7 were resistant to pain suggesting that Nav1.7 could be a target for the development of novel analgesic. ProTx-II, a peptide toxin belonging to the inhibitory cystine knot (ICK) family, was shown to selectively block the Nav1.7 channel but lacked in vivo efficacy.
Oligomerization, albumin binding and catabolism of therapeutic peptides in the subcutaneous compartment: an investigation on lipidated GLP-1 analogs
We are delighted to publish our first paper of 2022 in the Journal of Pharmaceutical and Biomedical Analysis (Elsevier). Here we leveraged our peptide #ADME toolbox to gain a better understanding of the interplay between oligomerization, albumin binding and catabolism of lipidated peptides in the subcutaneous compartment, using #GLP-1 analogs as model peptides.