Sonia Contel

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

Back to back publications on self-assembing peptide polymers

Polymerization-Induced Self-Assembly (PISA) concept is based on the chain extension of homopolymers with a co-monomer to yield asymmetric block copolymers. During the chain extension with the second block, self-assembly is induced by the insolubility of the second block in the polymerization solution.

Self-assembling peptides (SAP) are a category of peptides, which undergo spontaneous assembling into ordered nanostructures.

In collaboration with ICGM and IEM institutes were the first to combine both strategies in order to obtain Self-Assembling Peptide—Polymer Nano-Objects via Polymerization-Induced Self-Assembly or SAP-PISA. In a first time SAP-PISA allowed us to obtain a range of original morphologies and macro architectures.

The way is open now for more structural exploration as well as for applications such as drug delivery.

Check more @

Self-Assembling Peptide—Polymer Nano-Objects via Polymerization-Induced Self-Assembly, Dao, L Vezenkov, G Subra, M.Amblard, M In, J-F Le Meins, F Aubrit, M-A Moradi, V Ladmiral, and M. Semsarilar* Macromolecules 2020, 53, 16, 7034–7043, https://doi.org/10.1021/acs.macromol.0c01260

Nano-assemblies with core-forming hydrophobic polypeptide via polymerization-induced self-assembly (PISA), T Dao, L Vezenkov, G Subra, V Ladmiral, M Semsarilar, Polym. Chem., 2020, Advance Article, DOI: 10.1039/D0PY00793E

Self-Assembling Peptide—Polymer Nano-Objects via Polymerization-Induced Self-Assembly

Macromolecules 2020, 53, 16, 7034–7043 https://doi.org/10.1021/acs.macromol.0c01260

Dao T,  Vezenkov L, Subra G, Amblard M, In M, Le Meins J-F, Aubrit F, Moradi M-A, Ladmiral A, Semsarilar M*

 

Abstract

Self-assembling peptides (SAPs) have been extensively studied for their ability to form nanoscale ordered structures driven by noncovalent molecular interactions. Meanwhile, polymerization-induced self-assembly (PISA) has been exploited as a facile and efficient way to produce various amphiphilic block copolymer nano-objects, whose self-assembly was governed predominantly by the interactions of the different blocks with the polymerization medium. In this work, we combined PISA with SAPs to prepare novel peptide–polymer hybrid nano-objects, thus harnessing the advantages of PISA and the self-assembling driving force of SAPs. A tripeptide methacrylamide derivative (MAm-Gly-Phe-Phe-NH2, denoted as MAm-GFF, where MAm means methacrylamide) was copolymerized with glycerol monomethacrylate (GMA) to produce a P(GMA65stat-(MAm-GFF)7) macro-chain transfer agent (macro-CTA) by reversible addition–fragmentation chain transfer polymerization in dimethylformamide. This peptide-based macro-CTA was then successfully chain-extended with poly(2-hydroxypropyl methacrylate) (PHPMA) by aqueous dispersion PISA, forming P(GMA65stat-(MAm-GFF)7)-b-PHPMA28 self-assembled objects. Fibrous structures were observed by transmission electron microscopy (TEM) and Cryo-TEM, in agreement with depolarized dynamic light scattering, static light scattering, and small-angle X-ray scattering experiments that also revealed long anisotropic morphologies. Such structures have not been reported previously for PISA-prepared nano-objects. This confirms the decisive influence of the GFF SAP on the self-assembly. In addition, annealing the PISA suspension at different temperatures led to a significant size decrease in the self-assembled objects and to a morphological transition caused by the thermosensitivity of both the core-forming PHPMA block and the stabilizing P(GMA-stat-(MAm-GFF)) block.

New paper in European Polymer Journal !

Through a collaboration with the biopolymer team of IBMM , the peptide team describes for the first time the preparation of peptide-nylons hybrids. This novel work add another example of polymer-peptide to the list of studies lead by IBMM peptide team including peptide-silicone, peptide-NCA polymerization and Serine based switchable polymers obtained by ring opening polymerization of lactones.
Special congratulation to all the successive students, post-docs and colleagues who performed this long-lasting experimental work which started in 2016!

Turning peptides into bioactive nylons

European Polymer Journal 2020. doi: 10.1016/j.eurpolymj.2020.109886

Said Jebors, Coline Pinese, Titouan Montheil, Audrey Bethry, Simon Verquin, Louise Plais, Marie Moulin, Chloé Dupont, Xavier Garric, Ahmad Mehdi, Jean Martineza and Gilles Subra.

 

 

Abstract

New synthetic textiles with physical and/or biological properties are increasingly used in medical applications.While a simple textile coating is usually carried out to obtain biological properties, covalent grafting should be considered for long-term applications. Herein, we have developed a new hybrid bioactive nylon whose synthesis involves a peptide sequence with a diacyl derivative. Numerous types of peptide-nylons were prepared by varying the molar percentage (0.1 %, 1 % and 10%) and orientation of the peptide in the polymer backbone. Nylons incorporating antibacterial peptides significantly inhibited S. aureus proliferation whereas nylons functionalized with cell-adhesive peptide enhanced the proliferation of L929 fibroblast. These results show that the incorporation of the peptides directly into the nylon skeleton is efficient and provides biological properties that suggest new ways of functionalizing biomedical textiles

Congratulations to Titouan who defended his PhD in February 2020 !

Titouan defended his PhD on February 14, 2020. He presented his work on the design of hybrid hydrogels for biomaterials applications.

New paper in ACS Omega journal !

Titouan, Laurine and Gilles published a paper on 3D sol-gel bioprinting in ACS Oméga journal. This work discribe the design of a multifunctional bioink from silylated HPMC and its bioprinting in the presence of cells during the sol-gel process.

Congratulations to Laurine who defended her PhD in November 2019 !

Laurine Valot finally presented her PhD work on the development of multifunctional hybrid hydrogels for cartilage repair with mesenchymal stem cells encapsulation. Her PhD was supervised by Pr. Gilles SUBRA from the peptide team and Pr. Ahmad MEHDI from Institut Charles Gerhardt in Montpellier.

Laurine presented at the 3rd workshop “Biofabrication & Cancer”

Laurine presented her PhD work and a shared project with Gilles Subra and Pr. Raphael Devillard and Dr. Adrien Naveau from BioTis laboratory in Bordeaux, on Sol-gel chemistry applied to 3D bioprinting: use of extrusion and LIFT-printing for the biofabrication of an oral carcinoma model. The workshop was organized by the Cancéropôle Grand Sud Ouest in September 2019 in Montpellier.

Congratulations to Laurine to published a first paper based on her PhD work !

The first publication of Laurine based on her PhD work has been published in ChemPlusChem.

We demonstrated that sol-gel process is actually a real bio-orthogonal reaction by using a co-catalysis at physiological pH.

See https://onlinelibrary.wiley.com/doi/full/10.1002/cplu.201900509

New paper in Materials Today Communications

Dealing with biorthogonal methods, the bibliography of the PhD of Cécile Echalier is now published as a comprehensive review in Materials Today Communications

See https://www.sciencedirect.com/science/article/pii/S2352492819302107