Author: Lubomir Vezenkov

Sonia Contel

Sonia

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.

 

Contact:
sonia.cantel@umontpellier.fr
+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

Prospect of Thiazole-based gamma-Peptides Foldamers in Enamine Catalysis: Exploration of the Nitro-Michael Addition

Chemistry. 2019 May 28;25(30):7396-7401. doi: 10.1002/chem.201901221. Epub 2019 May 7.

Aguesseau-Kondrotas J, Simon M, Legrand B, Bantigniès JL, Kang YK, Dumitrescu D, Van der Lee A, Campagne JM, de Figueiredo RM, Maillard LT.

Abstract

As three-dimensional folding is prerequisite to biopolymer activity, complex functions may also be achieved through foldamer science. Because of the diversity of sizes, shapes and folding available with synthetic monomers, foldamer frameworks enable a numerous opportunities for designing new generations of catalysts. We herein demonstrate that heterocyclic γ-peptide scaffolds represent a versatile platform for enamine catalysis. One central feature was to determine how the catalytic activity and the transfer of chiral information might be under the control of the conformational behaviours of the oligomer.

IBMM peptide promoting science to highschool teachers!

Team Peptide is involved with vulgarisation of science ! It was our pleasure and privilege to receive eight high school teachers from the south of France reagion! At the pictures Laurine Valot, Gilles Subra and Lubomir Vezenkov animating a workshop on 3d printing of peptide materials and solid phase peptide synthesis.

A new ultra high performance equipment for IBMM and our team!

IBMM has recently acquired this wonderful UPLC and mass-spectrometry toy! It is an Aquity Hclass UPLC (Pierre Sanchez to the left, the engeneer that operates it) produced by Waterstm that can sustain the amazing 15000 psi! While other HPLC would crumble under such pressure this fine equipment provides an amazing HPLC separation! Getting to 95% purity just got harder in our team!

Marcrilen approved by the The European Medicines Agency!

The European Medicines Agency (EMA) has granted marketing authorization for MacrilenTM (JMV 1843), an orally available ghrelin agonist developed in our team ! Macrilen is used for diagnosis of adult growth hormone deficiency (AGHD). The approval came following the Committee for Medicinal Products for Human Use (CHMP) positive opinion of MacrilenTM.

People who have AGHD can include those who were GH deficient as children and become adults with AGHD, or adults who become GH deficient. In adults, GH deficiency could develop when your pituitary gland or hypothalamus is damaged due to tumors, surgery, radiation, or traumatic brain injury. GH is important for adults to support healthy tissue and organs. GH is released in pulses, so measuring your blood for too little GH (also known as a deficiency) may be hard. MacrilenTM, orally administered, will stimulate GH secretion in the circulation, which level can then be evaluated by simple blood samples.

Synthesis of Peptide–Adenine Conjugates as a New Tool for Monitoring Protease Activity

Eur. J. Org. Chem. January 2019: 176-183. doi:10.1002/ejoc.201801490.

Masurier, N. , Soualmia, F. , Sanchez, P. , Lefort, V. , Roué, M. , Maillard, L. T., Subra, G. , Percot, A. and El Amri, C.

Abstract

We took advantage of the powerful adenine SERS (Surface Enhanced Raman Spectroscopy) probe to design peptide–adenine conjugates as candidates for use as serine protease substrates. Whereas the direct introduction of the peptide sequence on the adenine exocyclic N6 amine gave an imidazopurinone derivative, the introduction of an aminoethyl linker between the adenine group and the peptide chain led to the expected candidate probes. These potential substrates were then evaluated for monitoring the hydrolytic activity of trypsin, used as a model protease, by HPLC and by SERS. We demonstrated that the Boc–VPR–adenine conjugate is a substrate of trypsin and constitutes a good starting point to design optimized substrates to monitor protease activity by SERS.

How are 1,2,3-triazoles accommodated in helical secondary structures?

Org Biomol Chem. 2018 May 15. doi: 10.1039/c8ob00686e

Ben Haj Salah K, Das S , Ruiz N , Andreu V , Martinez J , Wenger E , Amblard M , Didierjean C , Legrand B , Inguimbert N

Abstract

1,4-Disubstituted-1,2,3-triazole (Tz) is widely used in peptides as a trans-amide bond mimic, despite having hazardous effects on the native peptide activity. The impact of amide bond substitution by Tz on peptide secondary structures is scarcely documented. We performed a Tz scan, by systematically replacing peptide bonds following the Aib residues with Tz on two model peptaibols: alamethicin F50/5 and bergofungin D, which adopt stable α- and 310 helices, respectively. We observed that the Tz insertion, whatever its position in the peptide sequences, abolished their antimicrobial activity. The structural consequences of this insertion were further investigated using CD, NMR and X-ray diffraction. Importantly, five crystal structures that were incorporated with Tz were solved, showing various degrees of alteration of the helical structures, from minor structural perturbation of the helix to partial disorder. Together, these results showed that Tz insertions impair helical secondary structures.