Main Conference Day 2 - Europe/Amsterdam
- David Craik, PhD - Professor of Biomolecular Structure, University of Queensland
We have demonstrated that cys-rich miniproteins (“knottins”) can be inserted into the CDR loops of an antibody to create a fusion molecule combining the specificity of the knottin and the benefits of an antibody. The format facilitates the use of phage display technology to engineer the affinity and specificity of the knottin. This will be exemplified using a variety of ion channel modulating knottins
- John McCafferty, PhD - Chief Technology Officer, Maxion Therapeutics
We screened a library of 3.2 million cyclic peptides intracellularly using SICLOPPS. Following a high throughput phenotypic screen we identified CP25, which displays synthetic lethality to MTAP deletion cells via the axis of metabolic vulnerability. Target ID work has identified on target effects, via RNA processing enzymes. We anticipate that our workflow can be applied to a variety of diseases, greatly accelerating the rate of drug discovery.
- Monika Papayova - EPSRC Doctoral Prize Research Fellow, University of Southampton
Fibrosis is a hallmark of many chronic diseases, associated to nearly 45% of all deaths in the industrialized world. Despite its significant impact on global health, effectively delivering therapeutics to these tissues remains challenging. This talk will discuss a novel targeting modality, offering a new perspective on drug-delivery to fibrotic tissues.
- Brenno Masina - Senior Graduate Student, ETH Zurich
Posttranslational modifications (PTMs) have a critical role in shaping peptide structure and function. This talk highlights conotoxins as model small, structured bioactive peptides to explore how PTMs influence folding, stability, and biological activity. Insights from these systems inform rational peptide design, and synthesis of modified peptides to understand and harness their biological activities.
- Anne Conibear, BSc(Hons) MSc PhD - Assistant Professor, Peptide and Protein Chemistry, Technische Universität Wien
α-Conotoxin Vc1.1 is a disulfide-rich peptide and a promising drug candidate for treating neuropathic and chronic pain. Backbone cyclisation was applied to enhance its drug-like properties, resulting in improved serum stability and oral bioavailability. However, this modification also adversely affected its stability and activity in simulated intestinal fluid (SIF). To address these adverse effects, we explored the use of polyethylene glycol (PEG) linkers as substitutes for peptide backbone cyclization linkers.
- David Craik, PhD - Professor of Biomolecular Structure, University of Queensland
Radioligand therapy (RLT) employs radioactive atoms linked to targeting peptide-based ligands to deliver radiation directly to cancer cells. In this presentation we will explores the principles of this innovative way of using peptides to treat cancer and also CMC challenges and opportunities.
- John Lopez, PhD - Associate Director Science & Technology, Novartis
Aligning requirements between pre-clinical peptide process development, CMC strategy foundation and risk-mitigated tox/Phase I package is the driving force at PolyPeptide. Modern High-throughput and intensified process tools are structuring our offering in the current, fast-moving environment for peptides. Right the first time, reliability and reproducibility for fast transition to clinic are success criteria for shortening time to IND. Our presentation will highlight our technical and commercial platform for peptide development and present technical case studies and examples of IND acceleration for various peptide programs.
- Victoire Laude - Innovation Scientist, PolyPeptide Laboratories
- Fabien Rousset, PhD - Global Director of Innovation, Polypeptide Group
In the early phase of drug development for peptide APIs, speed to start Phase I is absolute key. With our early phase development concept, including process and analytical development, we can strongly reduce the time to manufacturing Tox and first GMP material. Synchronized timelines and parallel workflows between drug substance and drug product within our PepCellerate™ platform allows to save time while reducing risks. A case study will be presented.
- Tobias Kapp, PhD - Global Head of Peptide Development, CordenPharma
Disulfide bond formation is a key step in the manufacture of cysteine‑containing peptides, yet established oxidation methods frequently rely on hazardous reagents such as iodine or hydrogen peroxide. These approaches can introduce safety concerns, material compatibility issues, limited scalability, and undesired side reactions including over‑oxidation and oligomer formation. We describe a new oxidation platform based on dehydroascorbic acid (DHA), the oxidized form of vitamin C, as a mild, selective, and sustainable reagent for disulfide bond formation. The method supports efficient oxidation under aqueous conditions and is compatible with both high‑concentration in‑solution processing and an integrated on‑column implementation during preparative HPLC purification. DHA‑mediated oxidation shows a consistently favorable impurity profile and avoids common side reactions observed with conventional oxidants, even for peptides with limited solubility or high aggregation propensity. The DHA‑based platform simplifies process design by enabling higher working concentrations, reducing unit operations, and allowing oxidation to be integrated into existing purification workflows. The use of a non‑hazardous, vitamin‑derived reagent improves operational safety and equipment compatibility while significantly lowering process mass intensity and solvent consumption. Together, these features support robust scale‑up and align peptide manufacturing with modern sustainability expectations, making the technology well suited for both late‑stage development and commercial production.
- Alexander Kleinsmann, PhD - Director R&D, CMC Development, Bachem AG
This presentation describes the end‑to‑end process development of Dapiglutide, highlighting how innovative manufacturing optimization increased overall yield from ~20% to over 60% and enabled robust, scalable, and industrially viable peptide manufacturing from laboratory to large‑scale production.
- Federico Di Chiaro - Senior CMC Project Manager, Zealand Pharma
- Carolin Lechner, PhD - Director R&D, Bachem
When the world needs millions of doses of a molecule transforming the treatment of type 2 diabetes and obesity — manufactured to the highest quality standards — manufacturing science becomes a contact sport. This talk draws on the real process challenges of tirzepatide manufacture to extract transferable principles about innovating under pressure — from bench anomaly to breakthrough, and from gram to metric ton.
- Stephanie Coffin - Global Peptide Drug Substance Steward, Eli Lilly

