Date of birth : 05/07/1975 ; Nationality : French
Researcher unique identifier : ORCID 0000-0001-8870-5635
I am at the forefront of innovation in the lab to discover new chemical ligation reactions for protein synthesis and modification.
I set up the development of SEA chemistry and did the total chemical synthesis of proteins under redox control. (Org. Lett. 2010 DOI , Angewandte Chemie Int. Ed. 2012 DOI , J. Pep. Sci. 2013 DOI ).
I participated in the understanding of hepatocyte growth factor/MET receptor activation determinants by chemically producing the kringle 1 domain of HGF/SF, the ligand of MET receptor. (Angewandte Chemie Int. Ed. 2012 DOI, J., Chem. Sci 2015 DOI ). The design of a strong MET agonist is currently in progress for regenerative medicine, in collaboration with E. Gherardi’s team in Pavia, Italy.
EDUCATION
1998 – Master in Organic Chemistry. University of Haute-Alsace, Mulhouse, France.
1998 – Engineer from Ecole Nationale Supérieure de Chimie de Mulhouse, France.
CURRENT POSITION
Since 2006 – Research Engineer, Pasteur Institute of Lille, France.
PREVIOUS POSITION
1998-2006 – Studies Engineer, Pasteur Institute of Lille, 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, 2696-2700. DOI We achieved accelerations for peptide bond formation using lower catalyst loading by engineering electrostatic interactions between the catalyst and the peptide reactants. |
| 2 | Agouridas, V.; Ollivier, N.; Vicogne, J.; Diemer, V.; Melnyk, O. (2022). Redox-controlled chemical protein synthesis: sundry shades of latency. Acc. Chem. Res., 55, 2685-2697. DOI An account of our work on the chemical synthesis of proteins using redox controlled chemical systems. |
| 3 | 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, 6667. DOI We achieved outstanding accelerations for peptide bond formation by engineering electrostatic interactions in the peptide reactants. |
| 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 | Ollivier, N. ; Toupy, T. ; Hartkoorn, R.C. ; Desmet, R. ; Monbaliu, J.C.M. ; Melnyk, O. (2018). Accelerated microfluidic native chemical ligation at difficult amino acids toward cyclic peptides. Nat. Commun., 9, 2847. DOI We designed a microfluidic system which enables cyclisation of peptides at difficult junctions in a few minutes. |