Date of birth: 13/04/1979; Nationality: French
Researcher unique identifier: 0000-0002-5735-4630
My research focuses on the development of novel synthetic strategies that facilitates, in terms of rate and number of chemical steps, the access to biologically relevant proteins.
I developped new cysteine surrogates that enable the total chemical synthesis of linear or cyclic proteins under redox control (Acc. Chem. Res. 2022 DOI, J. Org. Chem. 2022 DOI, Methods in Molecular Biology DOI, Nat. Commun. 2020 DOI).
I contributed to the design of catalytic approaches that accelerate the ligation of peptide segments in water. (Org. Lett. 2023 DOI, J. Org. Chem. 2018 DOI)
EDUCATION
2007 PhD “Synthesis of zwitterionic biaryls for SAR in nonlinear optics”. University of Haute-Alsace, Mulhouse, France.
2003 Master in Organic Chemistry. University of Haute-Alsace, Mulhouse, France.
2003 Engineer’s degree. Ecole Nationale Supérieure de Chimie de Mulhouse, France.
CURRENT POSITION
Since 2018 CNRS researcher, Lille, France.
PREVIOUS POSITIONS
2016-2018 Post-doc in Dr O. Melnyk team “Total synthesis of cyclic proteins”
Lille, France
2014-2015 Post-doc in Dr G. Guichard team “Oligoureas as new organocatalysts”
Bordeaux, France.
2011-2014 Post-doc in Pr J. Clayden team “Design and synthesis of poly-Aib peptide helices”
Manchester, England.
2008-2010 Post-doc in Dr F. Leroux team “Development of the ARYNE coupling”
Strasbourg, France.
SELECTION OF FIVE RECENT PUBLICATIONS
| 1 | Ollivier, N.; Roy, E.; Desmet, R.; Agouridas, V.; Diemer, V.; Melnyk, O. (2023) Electrostatic Assistance of 4-Mercaptophenylacetic Acid-Catalyzed Native Chemical Ligation. Org. Lett. 25, 15, 2696. DOI We achieved accelerations for peptide bond formation using lower catalyst loading by engineering electrostatic interactions between the catalyst and the peptide reactants. |
| 2 | Firstova, O.; Melnyk, O.; Diemer, V. (2022). Thiol catalysis of selenosulfide bond cleavage by a triarylphosphine. J. Org. Chem. 87, 14, 9426. DOI We discovered that selenosulfide bond in model peptide sequences are efficiently cleaved by water-soluble aromatic phosphines in the presence of thiol. |
| 3 | Agouridas, V.; Ollivier, N.; Vicogne, J.; Diemer, V.; Melnyk, O. (2022) Redox-controlled chemical protein synthesis: sundry shades of latency. Acc. Chem. Res. 55, 2685. DOI An account of our work on the chemical synthesis of proteins using redox controlled chemical systems. |
| 4 | 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. |
| 5 | Cargoët, M.; Diemer, V.; Snella, B.; Desmet, R.; Blanpain, A.; Drobecq, H.; Agouridas, V.; Melnyk O. (2018) Catalysis of thiol-thioester exchange by water-soluble alkyldiselenols applied to the synthesis of peptide thioesters and SEA-mediated ligation. J. Org. Chem. 83, 20, 12584. DOI We designed novel water-soluble catalysts that accelerate key processes used in protein chemical synthesis, i.e., thiol-thioester exchange and amide bond formation reactions. |