Oleg Melnyk
Protein total synthesis

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The power of solid phase protein chemical synthesis for accessing challenging proteins. Chemical Science 2017, in press

The Protein Chemical Synthesis (PCS) database has been launched!

Chemistry is everywhere!

SeEA latent selenoesters and total synthesis of NK1 protein (180 AA). Raibaut, L. et al. Chem. Sci. 2016 DOI: 10.1039/C5SC03459K

Solid Phase Peptide & Protein Synthesis

Semi-synthesis of a HGF/SF kringle one (K1) domain scaffold generates a potent in vivo MET receptor agonist Simonneau, C. et al. Chem. Sci. 2015, 6, 2110-2121.

One-pot chemical synthesis of small ubiquitin-like modifier (SUMO) protein-peptide conjugates using bis(2-sulfanylethyl)amido peptide latent thioester surrogates. Boll, E. et al. Nat. Protocols 2015, 10, 269-292.

Access to large cyclic peptides by a one-pot two-Peptide segment ligation/cyclization process. Boll, E. et al. Org. Lett. 2015, 17, 130-133.

Solid phase protein synthesis. Raibaut, L. et al. Topics Curr. Chem. 2015, 363, 103-154.

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Chemical Science paper out

published on , updated on

Chemical protein synthesis gives access to well-defined native or modified proteins that are useful for studying protein structure and function. The majority of the proteins synthesized up to now were produced using native chemical ligation (NCL) in solution. Although there are significant advantages for assembling large peptides or proteins by solid phase ligation, works that reported such approaches are rare. We report a novel solid phase method for protein synthesis which relies on the chemistry of acetoacetyl group and ketoxime ligation for the attachment of the peptide to the solid support, and on a tandem transoximation/rearrangement process for the detachment of the target protein. Importantly, we show that the combination of solid phase and solution ligation techniques facilitates the production of a challenging and biologically active protein made of 180 amino acids. We show also that the solid phase method enables the purification of complex peptide segments through a chemoselective solid phase capture/release approach.

A simple and traceless solid phase method simplifies the assembly of large peptides and the access to challenging proteins
Ollivier, N., Desmet, R., Drobecq, H., Blanpain, A., Boll, E., Leclercq, , Mougel, A., Vicogne, J. and Melnyk, O. Chem. Sci. 2017 in press
DOI: 10.1039/C7SC01912B


published on , updated on

The Protein Chemical Synthesis (PCS) database has been launched and can be consulted on a dedicated website: http://pcs-db.fr
Native chemical ligation and extended methodologies are the most popular chemoselective reactions for protein chemical synthesis. Their combination with desulfurization techniques can give access to small or challenging proteins that are exploited in a large variety of research areas. In this report, we have conducted a statistical review of their use for protein chemical synthesis in order to provide a flavor of the recent trends and identify the most popular chemical tools used by protein chemists. To this end, a Protein Chemical Synthesis (PCS) database was created by collecting a set of relevant data from more than 450 publications covering the period 1994-2017.

Oleg Melnyk will attend the next Iberian Peptide Meeting as an invited speaker. It is organized in the auditorium of the Barcelona Biomedical Research Park (PRBB) from the 5th to the 7th of February, 2018. This meeting is designed to assemble the Iberian (Spanish-Portuguese) peptide community along with the Spanish Chemical Biology community into an international conference.