The scientists presenting in the March webinar will be Dr Nina Hartrampf, Assistant Professor at the University of Zurich, and Dr Nicola Wade, PDRA in the Jamieson Group at the University of Glasgow.
Date: 06-03-2026
Time: 1:00-2:00 pm
Venue: an online Zoom seminar
Dr Nina Hartrampf, Assistant Professor in the Department of Chemistry at the University of Zurich
Title: Deciphering Phosphorylation-Dependent MYC Interactions with Chemical Protein Synthesis
The protein MYC is an intrinsically disordered transcription factor that is upregulated in more than 50% of cancers and engages in numerous protein鈥損rotein interactions. Many of its interactions are frequently regulated by post-translational modifications (PTMs) of the transactivation domain (TAD), most commonly through (poly)phosphorylation. Investigating these modifications at the molecular level requires protein samples with defined and site-specific PTM patterns, which can be accessed through chemical peptide and protein synthesis. More specifically, we use flow-SPPS at elevated temperatures, which enables the routine synthesis of longer peptides and provides additional insight into the synthesis process itself. In this presentation, the concept of flow-based protein synthesis will be introduced, and our efforts to decipher MYC鈥檚 phosphorylation-dependent protein鈥損rotein interactions will be highlighted. A crucial first step toward this goal was the synthesis of MYC鈥檚 TAD, a so-called 鈥渄ifficult sequence鈥� that is challenging to access and therefore prompted the development of new, broadly applicable tools for chemical protein synthesis.
Dr Nicola Wade, PDRA in the Jamieson Group at the University of Glasgow School of Chemistry.
Title: Expanding the scope of sustainable peptide synthesis through post-linear synthesis reactions
The replacement of N,N-dimethylformamide (DMF) in solid-phase peptide synthesis (SPPS) is critical for improving the sustainability and safety of peptide research. While N-butyl-2-pyrrolidinone (NBP) has emerged as a viable alternative for linear peptide synthesis, its applicability to post-linear synthesis modifications remains underexplored. Here, we demonstrate the use of NBP as an alternative solvent for key on-resin transformations required in peptidomimetic synthesis, including orthogonal protecting group removal and on-resin peptide cyclisation strategies. We will present our findings, establishing NBP as a practical and greener alternative to DMF for diverse post-linear synthesis modifications, supporting the development of sustainable SPPS protocols.
Date: 06-03-2026
Time: 1:00-2:00 pm
Venue: an online Zoom seminar
Dr Nina Hartrampf, Assistant Professor in the Department of Chemistry at the University of Zurich
Title: Deciphering Phosphorylation-Dependent MYC Interactions with Chemical Protein Synthesis
The protein MYC is an intrinsically disordered transcription factor that is upregulated in more than 50% of cancers and engages in numerous protein鈥損rotein interactions. Many of its interactions are frequently regulated by post-translational modifications (PTMs) of the transactivation domain (TAD), most commonly through (poly)phosphorylation. Investigating these modifications at the molecular level requires protein samples with defined and site-specific PTM patterns, which can be accessed through chemical peptide and protein synthesis. More specifically, we use flow-SPPS at elevated temperatures, which enables the routine synthesis of longer peptides and provides additional insight into the synthesis process itself. In this presentation, the concept of flow-based protein synthesis will be introduced, and our efforts to decipher MYC鈥檚 phosphorylation-dependent protein鈥損rotein interactions will be highlighted. A crucial first step toward this goal was the synthesis of MYC鈥檚 TAD, a so-called 鈥渄ifficult sequence鈥� that is challenging to access and therefore prompted the development of new, broadly applicable tools for chemical protein synthesis.
Dr Nicola Wade, PDRA in the Jamieson Group at the University of Glasgow School of Chemistry.
Title: Expanding the scope of sustainable peptide synthesis through post-linear synthesis reactions
The replacement of N,N-dimethylformamide (DMF) in solid-phase peptide synthesis (SPPS) is critical for improving the sustainability and safety of peptide research. While N-butyl-2-pyrrolidinone (NBP) has emerged as a viable alternative for linear peptide synthesis, its applicability to post-linear synthesis modifications remains underexplored. Here, we demonstrate the use of NBP as an alternative solvent for key on-resin transformations required in peptidomimetic synthesis, including orthogonal protecting group removal and on-resin peptide cyclisation strategies. We will present our findings, establishing NBP as a practical and greener alternative to DMF for diverse post-linear synthesis modifications, supporting the development of sustainable SPPS protocols.
