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Our peptide chemistry team is excited to announce a new publication in the journal “Circulation”, which highlights the outcome of a highly successful drug discovery collaboration with Merck & co.’s world-class drug discovery group (Kenilworth, New Jersey).
The publication describes the discovery of a novel series of Imidazopyrazine derivatives by IRBM’s drug discovery team. This novel series of SHP2 allosteric inhibitors, having an imidazopyrazine 6,5-fused heterocyclic system as central scaffold, showed an excellent potency in enzyme and cellular assays.
Innovative synthetic strategies giving access to a larger chemical space are of great importance to make the development of peptide therapeutics a faster and more efficient process. Katritzky salts, easily prepared from primary amines, offer peptide chemists a tool to achieve many chemical transformations in a straightforward manner.
The IRBM peptide chemistry team is proud to announce a new publication in ACS Medicinal Chemistry Letters in collaboration with the outstanding drug discovery team at Merck & Co. (Kenilworth, NJ).
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.
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.
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.
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.
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