Main Conference Day 2Wednesday, 12 November 2025 - CET (Central European Time, GMT+01:00)

We report a programmable, pH-controlled strategy for site-selective cysteine modification in peptides using triazine-thiol exchange. Internal or N-terminal cysteines can be site-selectively modified via dynamic covalent chemistry. We have supported our mechanistic model with both, experimental and computational studies, enabling precision peptide engineering through tunable, mechanism-guided cysteine functionalization.

Protein–protein interactions (PPIs) represent promising but underexploited targets in drug discovery and development due to the challenging landscapes of their extensive contact interfaces. The identification of reactivity hotspots within these interfaces by electrophile scanning facilitates the design of covalently binding peptides with enhanced potential as PPI inhibitors.

Extracorporeal membrane oxygenation (ECMO) is a form of life support for critically ill patients with severe respiratory or cardiac failure. However, interactions between patient blood and ECMO biomaterials increase the risk of thrombosis, necessitating concurrent anticoagulation treatment, with the standard of care being heparin. Here we describe the use of mRNA display based discovery using a cyclotide scaffold to develop a factor XII inhibitor as a selective anticoagulant that offers a potential alternative to heparin in ECMO treatment.

This presentation will discuss how peptides unlock a completely new possibility for dissolving neurotoxic protein aggregates, which are a hallmark to various neurodegenerative disorders. The development of PRI-002 from discovery to phase II in Alzheimer’s disease will be presented.

Non-ribosomal peptides (NRPs) represent one of nature’s most powerful solutions for addressing complex biological challenges. These peptides exhibit rich structural diversity and possess properties that enable them to engage difficult therapeutic targets - including those inaccessible to traditional small molecules or biologics. NRPs are the foundation for several successful drugs, from immunosuppressants to antibiotics. At Myria Biosciences, we are building on these natural molecules to develop a next-generation drug discovery platform. Our approach begins with a simple premise: decode how nature builds chemistry. We curate and generate high-quality datasets from natural biosynthetic pathways and organisms, using them to train models that predict how modular NRP biosynthetic enzymes generate diverse chemical structures. These insights enable us to reprogram microbial hosts with custom-designed biosynthetic pathways, producing novel macrocyclic peptides not found in nature. Our platform combines synthetic biology, machine learning, and high-throughput experimentation. It enables the design, production, and screening of thousands of novel compounds per week. Because it operates in living systems, the platform supports rapid, scalable iteration and exploration of vast chemical space. In this talk, I will explain how Myria leverages NRP systems’ modular logic to build a scalable industrial platform, transforming nature’s biosynthetic language into an engine for precision drug discovery.

Solid Phase Peptide Synthesis (SPPS) is efficient but generates significant solvent waste. Tag-Assisted Peptide Synthesis (TAPS) offers a greener, solution-phase alternative using soluble tags. We present a continuous TAPS process using aqueous washes after each cycle in a green solvent system, reducing organic solvent use by 90% and reagent excess by >50%, while maintaining product quality—establishing TAPS as a sustainable alternative to SPPS.