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Dr Muriel AMBLARD is a CNRS Research Director at the “Institute of Biomolecules Max Mousseron” (IBMM) in France (Montpellier) in the Amino Acids, Peptides and Proteins Department. After completing her PhD in Organic Chemistry at the University of Montpellier in the laboratory of Prof Jean Martinez, she joined the group of Dr Paul Anderson at Merck Sharp & Dohm in the USA as a post-doctoral fellow. In 1996, she obtained a position at the Laboratory of Amino Acid Peptides and Proteins in Montpellier. She became a team leader at the IBMM in 2007 and was appointed deputy director of the IBMM in 2015. Her research interests are mainly at the interface of chemistry, biology and structural analysis for the development of bioactive compounds and peptide-based chemical tools that can mimic biological systems. Part of her research is also dedicated to the development of new methodologies in peptide synthesis (O-N acyl transfer reaction for the synthesis of cyclic peptides without epimerisation, new strategy for the synthesis of peptide alcohols on solid support, synthesis of stapled peptides and peptide-based biopolymers by new and original approaches based on bottom-up polymerisation of peptide-activated monomers). She has contributed to the development of potent GPCR agonists and antagonists of peptide hormones, in particular cholecystokinin and bradykinin. Her recent work has focused on the design and synthesis of constrained β-amino acid and dipeptide mimetic oligomers as highly predictable and stable helical molecular architectures (foldamers), as well as on stapled peptides. Both families of molecules are being used to develop specific therapeutic tools capable of inhibiting intracellular PPIs and as vectors for the intracellular delivery of bioactive molecules. Today, another part of her research interest is devoted to the development of selective protein degraders using Proteolysis-Targeting Chimeras (PROTACs) technology. Muriel is co-author of over 108 papers, 5 book chapters and 12 patents. 5 major publications : Kelly, LM et al. Targeting a lineage-specific PI3Kγ-Akt signaling module in acute myeloid leukemia using a heterobifunctional degrader molecule. Nature Cancer, 2024, doi: 10.1038/s43018-024-00782-5 Bourbiaux K., Legrand B., Verdié P., Mallart S., Manette G., Minoletti C., Stepp J.D., Prigent P., Le Bail JC., Gauzy-Lazo L., Duclos O., Martinez J., Amblard M. Potent Lys Patch-Containing Stapled Peptides Targeting PCSK9. J. Med. Chem. 2021, 12;64(15):10834-10848. doi: 10.1021/acs.jmedchem.0c02051 C. Bouclier, M. Simon, G. Laconde, M. Pellerano, S. Diot, S. Lantuejoul, B. Busser, L. Vanwonterghem, J. Vollaire, V. Josserand, B. Legrand, J.L. Coll, M. Amblard, A. Hurbin, M. C. Morris. Stapled peptide targeting the CDK4/Cyclin D interface synergizes with Abemaciclib in non-small cell lung cancers, Theranostics 2020; 10(5):2008-2028 Martin, B. Legrand, L. L. Vezenkov, M. Berthet, G. Subra, M. Calmès, J.L. Bantignies, J. Martinez, M. Amblard. Turning peptide sequences into ribbon foldamers via a straightforward multi-cyclization reaction. Angew. Chem. Int. Ed., 2015, 54, 13966 –13970