Nationality: French
Researcher unique identifier: ORCID 0000-0003-0911-1527
My research activities are focused on the chemistry of peptide thioesters and the native chemical ligation reaction (NCL) for protein synthesis and modification. They are deployed from development to application, including a mechanistic understanding of the approaches developed.
Methodological developments : discovery and optimization of ligation systems through the application of new chemical reactivities (Chem. Rev. 2019 DOI, Angew. Chem. Int. Ed. 2022 DOI, Nat. Commun. 2022 DOI, Acc. Chem. Res. 2022 DOI)
Total chemical synthesis of proteins: validation of the robustness of the developed methods through the total synthesis of one or more large demonstrators, most often in connexion with a biological problem (Molecules 2021 DOI, Org. Lett. 2023 DOI).
Development of bibliographic analysis tools and computational approaches: Development of decision support tools for protein synthesis (Bioorg. Med. Chem. 2017 DOI, creator and webmaster of the Protein Chemical Synthesis database PCS : pcs-db.fr) and kinetics-based mechanistic analysis of ligation reactions (J. Org. Chem. 2018 DOI, Nat. Commun. 2020 DOI)
I teach organic chemistry at Centrale Lille-ENSCL from bachelor to master degrees (this includes classical reactivity, reactivity of biomolecules, heterocyclic chemistry, enzymatic catalysis… for an overall volume of ~250 h / academic year).
EDUCATION
2021 Habilitation thesis to supervise research.
2006 PhD “Design, synthesis and biological evaluation of fluorinated analogues of steroidal antiestrogens”, University Versailles Saint-Quentin, Versailles, France.
2003 Master « Fluorinated analogues of Tamoxifen », University Versailles Saint-Quentin, Versailles, France.
CURRENT POSITION
Since 2020 Assistant Professor at Centrale Lille-ENSCL, Lille, France
PREVIOUS POSITIONS
2009-2020 Assistant Professor at Ecole Nationale Supérieure de Chimie Lille, Lille, France
2008-2009 Post-doc “Lead optimization of a drug candidate”, Faculté de Pharmacie de Châtenay-Malabry, Paris XI, Paris, France
2007-2008 Post-doc “Total synthesis of discodermolide analogues”, Faculté de Pharmacie de Paris V, Paris, France
2006-2007 Post-doc “Total synthesis of cytotrienin A”, Boston University, Boston, USA
SELECTION OF FIVE RECENT PUBLICATIONS
| 1 | Desmet, R., Boidin-Wichlacz, C., Mhidia, R., Tasiemski, A., Agouridas, V., and Melnyk, O. (2023). An Iron-Catalyzed Protein Desulfurization Method Reminiscent of Aquatic Chemistry. Angew. Chem. Int. Ed. 62. e202302648. DOI A novel method for effecting the selective desulfurization of cysteine at the protein level, using an iron-catalyzed process reminiscent of aquatic chemistry. Hot Paper. |
| 2 | Ollivier, N., Sénéchal, M., Desmet, R., Snella, B., Agouridas, V., and Melnyk, O. (2022). A biomimetic electrostatic assistance for guiding and promoting N-terminal protein chemical modification. Nat. Commun. 13. 66667. DOI We achieved outstanding accelerations for peptide bond formation by engineering electrostatic interactions in the peptide reactants. |
| 3 | Snella, B.; Grain, B.; Vicogne, J.; Capet, F.; Melnyk, O.; Agouridas, V. (2022) Fast protein modification in the nanomolar concentration range using an oxalyl amide as latent thioester. Angew. Chem. Int. Ed. 61, e202204992. DOI Inspired by the very high reactivity of some cell metabolites, this work has potentially significant implications for the accelerated production of conjugates of medical interest. Hot Paper. |
| 4 | Agouridas, V.; Ollivier, N.; Vicogne, J.; Diemer, V.; Melnyk, O. Redox-controlled chemical protein synthesis: sundry shades of latency. Acc. Chem. Res. 2022, 55, 2685-2697. DOI An account of our work on the chemical synthesis of proteins using redox controlled chemical systems. |
| 5 | Diemer, V.; Ollivier, N.; Leclercq, B.; Drobecq, H.; Vicogne, J.; Agouridas, V.; Melnyk, O. (2020) A cysteine selenosulfide redox switch for protein chemical synthesis. Nat. Commun. 11, 2558. DOI – We designed a redox-controlled cysteine surrogate facilitating the chemical synthesis of complex protein scaffolds such as cyclic proteins. Article highlighted by the Editors of Nature Communications. |