Sonia Cantel

Sonia Cantel

Assistant Professor-HDR, Faculty of Sciences/ Faculty of Pharmacy, University of Montpellier

Sonia Cantel obtained her PhD in 2004 in Chemistry of Biomolecules from the University of Montpellier, under the supervision of Dr. J-A Fehrentz, in the field of pseudo-peptide and solid phase organic synthesis. Then, she joined the group of Pr. M. Chorev for the following two years as a Post-doctoral Fellow in the Laboratory for Translational Research (Harvard Medical School, Boston, USA). She actively participated to biomedicinal projects where chemistry plays a critical role but also required the input of other scientific disciplines. In this interdisciplinary research environment, she developped extensive skills in analytical techniques applied to protein engineering. Her accomplishments included development of new methodologies for synthesis of glycated antigenic peptides and in situ templated assembly of fragments to generate potent inhibitors of protein-protein interaction.

She joined in 2007 the group of Professor J. Martinez as an Assistant-Professor at the University of Montpellier in Mass Spectrometry, taking advantage of her multidisciplinary experience to develop new projects at the interface of Chemistry, Biology and Analytical Sciences.

She focuses her research on the development of chemical probes for specific and sensitive detection of peptides and proteins, and pharmacological studies (GPCR/ligand interaction) by MALDI Mass Spectrometry.

+33 (0)4 11 75 96 07

+33 (0)4 67 14 38 09

Major publications :

  1. “Quantitative MALDI-MS Binding Assays: An Alternative to Radiolabeling”, Rossato, G. Miralles, C. M’Kadmi, D. Gagne, M. Amblard, B. Mouillac, J. Martinez, G. Subra, C. Enjalbal and S. Cantel, ChemMedChem, 11 (23), 2582-2587 (2016) IF= 2.98
  2. “Angiotensin-Converting Enzyme is the target of the nonapeptide Acein that induces dopamine release” Neasta, C. Valmalle, A.C. Coyne, E. Carnazzi, G. Subra, J.C. Galleyrand, D. Gagne, C. M’Kadmi, N. Bernad, G. Bergé, S. Cantel, J. Marie, J.L. Banères, M.L. Kemel, V. Daugé, K. Puget, J. Martinez, British Journal of Pharmacology, 173, 1314-1328 (2015) IF= 4.84
  3. “An innovative Strategy for sulfopeptides analysis using MALDI-TOF MS reflectron positive ion mode” CANTEL, L. BRUNEL, K. OHARA, C. ENJALBAL, J. MARTINEZ, J.J. VASSEUR, M. SMIETANA*, Proteomics, 12, , 2247-2257 (2012). IF = 4,82
  4. “A new generation of cross-linkers for selective detection by MALDI MS”, D. PARAMELLE, CANTEL, C. ENJALBAL, M. AMBLARD, E. FOREST, M. HEYMANN, C. GEOURJON, J. MARTINEZ, G. SUBRA, Proteomics, 9, 5384-5388 (2009). IF = 4,82
  5. “Synthesis and Conformational Analysis of a Cyclic Peptide Obtained via i to-i+4 Intramolecular Side Chain-to-Side Chain Azide-Alkyne 1,3-Dipolar Cycloaddition”, CANTEL, A. LE CHEVALIER-ISAAD, M. SCRIMA, J.J. LEVI, R.D. DIMARCHI, P. ROVERO, J.A. HALPERIN, A.M. D’URSI, A.M. PAPINI, M. CHOREV, J. Org. Chem. (Featured Article), 73, 5663-5674 (2008). IF = 3,96
  6. “Small Molecule Inhibition of the Interaction Between the Translation Initiation Factors eIF4E and eIF4G”, N.J. MOERKE, H. AKTAS, H. CHEN, CANTEL, M.Y. REIBARKH, J.D. GROSS, A. DEGTEREV, J. YUAN, M. CHOREV, J.A. HALPERIN, G. WAGNER, Cell, 128, 257-267 (2007). IF = 29,89
  7. “Solution and solid-supported synthesis of 3,4,5-trisubstituted 1,2,4-triazole-based peptidomimetics” D. BOEGLIN, CANTEL, A. HEITZ, J. MARTINEZ, J.A. FEHRENTZ, Org. Lett., 5, 23, 4465-4468 (2003).  IF = 5,25


Recent publication with the group

  1. “N-terminal LEAP2 region exhibits inverse agonist activity toward the ghrelin receptor“, M’Kadmi, A. Cabral, F. Barrile, J. Giribaldi, S. Cantel, M. Damian, S. Mary, S. Denoyelle, S. Dutertre, S. Péraldi-Roux, J. Neasta, C. Oiry, J.L. Banères, J. Marie, M. Perello and J.A. Fehrentz , J. Med. Chem. in press (2018) IF= 6.25
  2. Receptor-ligand interaction measured by Inductively Coupled Plasma Mass Spectrometry and selenium labeling“, Cheignon, E. Cordeau, Nolwenn Prache, S. Cantel, J. Martinez, G. Subra, C. Arnaudguilhem, B. Bouyssiere, C. Enjalbal, (2018) J.Med.Chem., 61, 10173-10184 (2018) IF= 6.25

Structure and dynamics of G protein-coupled receptor-bound ghrelin reveal the critical role of the octanoyl chain

Proc Natl Acad Sci U S A. 2019 Aug 27;116(35):17525-17530. doi: 10.1073/pnas.1905105116. Epub 2019 Aug 15

Ferré G, Louet M, Saurel O, Delort B, Czaplicki G, M’Kadmi C, Damian M, Renault P, Cantel S, Gavara L, Demange P, Marie J, Fehrentz JA, Floquet N, Milon A, Banères JL.


Ghrelin plays a central role in controlling major biological processes. As for other G protein-coupled receptor (GPCR) peptide agonists, the structure and dynamics of ghrelin bound to its receptor remain obscure. Using a combination of solution-state NMR and molecular modeling, we demonstrate that binding to the growth hormone secretagogue receptor is accompanied by a conformational change in ghrelin that structures its central region, involving the formation of a well-defined hydrophobic core. By comparing its acylated and nonacylated forms, we conclude that the ghrelin octanoyl chain is essential to form the hydrophobic core and promote access of ghrelin to the receptor ligand-binding pocket. The combination of coarse-grained molecular dynamics studies and NMR should prove useful in improving our mechanistic understanding of the complex conformational space explored by a natural peptide agonist when binding to its GPCR. Such information should also facilitate the design of new ghrelin receptor-selective drugs.

Selenazolidine: A selenium containing proline surrogate in peptide science

Organic & Biomolecular Chemistry, 2016, Volume: 14, Issue: 34, Pages: 8101-8108, DOI: 10.1039/C6OB01450J

E. Cordeau, S. Cantel, D. Gagne, A. Lebrun, J. Martinez, G. Subra, C. Enjalbal 


In the search for new peptide ligands contg. selenium in their sequences, we investigated L-4-selenazolidine-carboxylic acid (selenazolidine, Sez) as a proline analog with the chalcogen atom in the γ-position of the ring.  In contrast to proteinogenic selenocysteine (Sec) and selenomethionine (SeMet), the incorporation within a peptide sequence of such a non-natural amino acid has never been studied.  There is thus a great interest in increasing the possibility of selenium insertion within peptides, esp. for sequences that do not possess a sulfur contg. amino acid (Cys or Met), by offering other selenated residues suitable for peptide synthesis protocols.  Herein, we have evaluated selenazolidine in Boc/Bzl (Boc = tert-butoxycarbonyl) and Fmoc/tBu (Fmoc = 9-fluorenylmethoxycarbonyl) strategies through the synthesis of a model tripeptide, both in soln. and on a solid support.  Special attention was paid to the stability of the Sez residue in basic conditions.  Thus, generic protocols have been optimized to synthesize Sez-contg. peptides, through the use of an Fmoc-Xxx-Sez-OH dipeptide unit.  As an example, a new analog of the vasopressin receptor-1A antagonist was prepd., in which Pro was replaced with Sez [3-(4-hydroxyphenyl)-propionyl-D-Tyr(Me)-Phe-Gln-Asn-Arg-Sez-Arg-NH2].  Both proline and such pseudo-proline contg. peptides exhibited similar pharmacol. properties and endopeptidase stabilities indicating that the presence of the selenium atom has minimal functional effects.  Taking into account the straightforward handling of Sez as a dipeptide building block in a conventional Fmoc/tBu SPPS strategy, this result suggested a wide range of potential uses of the Sez amino acid in peptide chem., for instance as a viable proline surrogate as well as a selenium probe, complementary to Sec and SeMet, for NMR and mass spectrometry anal. purposes.

Investigation of elemental mass spectrometry in pharmacology for peptide quantitation at femtomolar levels

PLoS One, 2016, Volume: 11, Issue: 6, Pages: e0157943/1-e0157943/18, DOI: 10.1371/journal.pone.0157943

E. Cordeau, C.  Arnaudguilhem, B. Bouyssiere, A. Hagege, J. Martinez,  G. Subra, S. Cantel, C. Enjalbal


In the search of new robust and environmental-friendly anal. methods able to answer quant. issues in pharmacol., we explore liq. chromatog. (LC) assocd. with elemental mass spectrometry (ICP-MS) to monitor peptides in such complex biol. matrixes.  The novelty is to use mass spectrometry to replace radiolabelling and radioactivity measurements, which represent up-to now the gold std. to measure org. compd. concns. in life science.  As a proof of concept, we choose the vasopressin (AVP)/V1A receptor system for model pharmacol. assays.  The capacity of ICP-MS to provide highly sensitive quantitation of metallic and hetero elements, whatever the sample medium, prompted us to investigate this technique in combination with appropriate labeling of the peptide of interest.  Selenium, that is scarcely present in biol. media, was selected as a good compromise between ICP-MS response, covalent tagging ability using conventional sulfur chem. and peptide detection specificity.  Applying selenium monitoring by elemental mass spectrometry in pharmacol. is challenging due to the very high salt content and org. material complexity of the samples that produces polyat. aggregates and thus potentially mass interferences with selenium detection.  Hyphenation with a chromatog. sepn. was found compulsory.  Noteworthy, we aimed to develop a straightforward quant. protocol that can be performed in any lab. equipped with a std. macrobore LC-ICP-MS system, in order to avoid time-consuming sample treatment or special implementation of instrumental set-up, while allowing efficient suppression of all mass interferences to reach the targeted sensitivity.  Significantly, a quantification limit of 57 ng Se L-1 (72 fmol of injected Se) was achieved, the samples issued from the pharmacol. assays being directly introduced into the LC-ICP-MS system.  The established method was successfully validated and applied to the measurement of the vasopressin ligand affinity for its V1A receptor through the detn. of the dissocn. const. (Kd) which was compared to the one recorded with conventional radioactivity assays.

Quantitative MALDI-MS Binding Assays: An Alternative to Radiolabeling

ChemMedChem, 2016, Volume: 11, Issue: 23, Pages: 2582-2587, DOI: 10.1002/cmdc.201600447

M. Rossato,  G. Miralles, C. M’Kadmi, M. Maingot, M. Amblard, B. Mouillac, D. Gagne, J. Martinez, G. Subra, C. Enjalbal, S. Cantel, 


Radiolabeling of ligands is still the gold std. in the study of high-affinity receptor-ligand interactions. In an effort toward safer and simpler alternatives to the use of radioisotopes, we developed a quant. and highly sensitive matrix-assisted laser desorption ionization mass spectrometry (MALDI-MS) method that relies on the use of chem. tagged ligands designed to be specifically detectable when present as traces in complex biol. mixts. such as cellular lysates. This innovative technol. allows easy, sensitive detection and accurate quantification of analytes at the sub-nanomolar level. After statistical validation, we were able to perform pharmacol. evaluations of G protein-coupled receptor (V1A-R)-ligand interactions. Both satn. and competitive binding assays were successfully processed.

Laser desorption ionization mass spectrometry of peptides on a hybrid CHCA organic-inorganic matrix

Journal of Proteomics, Volume, 2014, 108, Pages: 369-372,  DOI: 10.1016/j.jprot.2014.06.005

C. Fleith, S. Cantel, G. Subra, A. Mehdi, J. Ciccione, J. Martinez, C. Enjalbal


We report applications of new hybrid org.-inorg. silica based materials as laser desorption/ionization (LDI)-promoting surfaces for high-throughput identification of peptides.  The driving force of our work was to design a new material composed of a conventional MALDI matrix covalently attached to silica with a high org./inorg. ratio in order to improve the UV absorption by such LDI hybrid matrixes.  Amorphous CHCA-functionalized silica presenting an org. content up to 1.3 mmol g-1 (around 40% in wt. from TGA and elementary anal. measurements) gave very interesting LDI performances in terms of detection sensitivity as well as relative ionization discrepancy (spectral suppression) through the analyses of small synthetic peptide mixts. (550-1300 Da) taking CHCA and amorphous silica as model matrixes for control expts.