Poster Presentation 6th Modern Solid Phase Peptide Synthesis & Its Applications Symposium 2017

Chemoselectively induced cysteine-conjugation to unsaturated phosphonamidates for the side-selective generation of peptide-protein conjugates (#46)

Marc-André Kasper 1 2 , Maria Glanz 1 2 , Christian P. R. Hackenberger 1 2
  1. Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Berlin, BERLIN, Germany
  2. Department of Chemistry, Humboldt-Universität zu Berlin, Berlin, Germany

Chemoselective bioconjugation to cysteine residues is one of the most convenient protein modification strategies due to its highly nucleophilic properties and relatively low abundance. Although a lot of different chemical methods have been recently applied to modify sulfhydryl groups [1], a technique that combines high selectivity, stable linkage and ease of introduction of the thiol reactive moiety is still rarely found in the literature.

In our group, we have developed a series of P(III) compounds including phosphites and phosphonites that react chemoselectively with azides to form stable P(V)-conjugates such as phosphor- or phosphonamidates.[2] These Staudinger-type reactions were applied successfully to small molecules, dyes, polymers as well as unprotected peptides and proteins in the presence of several functional groups. Furthermore, we showed that alkyne-containing phosphonites can be used for a formal and modular conjugation of two azido-containing molecules.[3]

In the current presentation, we extend the use of such phosphorous reagents by the introduction of unsaturated phosphonamidates for the selective modification of Cys- residues. In a modular fashion, phosphonamidates can be introduced into unprotected peptides via the Staudinger-phosphonite reaction with azides. Solid-phase peptide synthesis allows the installation of aromatic and aliphatic azides, which can be selectively modified after cleavage from the resin. The first chemoselective Staudinger-reaction induces reactivity for the subsequent conjugation to thiols, which can be performed in aqueous buffers and proceeds with a unique selectivity. The resulting conjugates can be obtained in high yields and we observed a remarkable stability towards exchange with external thiols. Building upon this outstanding performance we were able to apply our method to the generation of novel peptide-linked, enhanced stability Antibody-Drug-Conjugates (ADCs) as well as functional cell-penetrating peptide-protein conjugates. [4]

  1. S. B. Gunnoo, A. Madder, ChemBioChem 2016, 17, 529-553.
  2. a) R. Serwa, I. Wilkening, G. Del Signore, M. Mühlberg, I. Claußnitzer, C. Weise, M. Gerrits, C. P. R. Hackenberger, Angew. Chem., Int. Ed. 2009, 48, 8234-8239; b) M. R. J. Vallée, P. Majkut, I. Wilkening, C. Weise, G. Müller, C. P. R. Hackenberger, Org. Lett. 2011, 13, 5440-5443; c) N. Nischan, A. Chakrabarti, R. A. Serwa, P. H. M. Bovee-Geurts, R. Brock, C. P. R. Hackenberger, Angew. Chem., Int. Ed. 2013, 52, 11920-11924.
  3. M. R. J. Vallée, L. M. Artner, J. Dernedde, C. P. R. Hackenberger, Angew. Chem., Int. Ed. 2013, 52, 9504-9508.
  4. M.-A. Kasper, M. Glanz, D. Schumacher, T. Sauer, C. P. R. Hackenberger, 2016, EP16 001 917.0.