All posts in none

Sponsored Talk by Asymchem
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Susan Li
Peptide Chief Scientist, CMC development and manufacturing, Asymchem Group

Forced Degradation Study of Peptides

Abstract

Peptides are a-amino acid polymers composed of 40 or fewer amino acids. Therapeutic peptides are less immunogenic and offering greater safety, selectivity and specificity. By understanding the degradation behavior of peptides, safer and more effective peptide drugs can be designed. Degradation studies are conducted including a selection of stress conditions, degradation products formed, and different peptide degradation mechanisms. A case study on the degradation profile of existing peptide drugs is presented as well.

Bio

Susan Li holds a PhD in Polymer Chemistry and Physics from Nankai University in China. She completed a postdoctoral fellowship at the University of Texas Southwestern Medical Center (UTSW) in the United States. Before joining Asymchem, she previously worked at PolyPeptide Group where she focused on CMC development for peptide APIs. She also served as a Senior Scientist in the Department of Macromolecular Life Sciences and Cancer Biology at the Stanford Research Institute (SRI), leading efforts to establish a peptide-targeted drug platform for cancer treatment and diagnosis. In 2019, Susan became the Director of Peptide R&D at Sinopep Biopharmaceutical Co., Ltd. in China, where she led the development of peptide APIs, including Semaglutide and Desmopressin. Under her leadership, the DMFs for these compounds were successfully completed and found to meet FDA standards. Currently, Susan works as the Peptide Chief Scientist at Asymchem Group, overseeing peptide CMC development and manufacturing.

Peptide Showcase
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Timothy Craven
CEO, Insamo

Integrating computational design and display screening for ultra high-throughput cell-permeable cyclic peptide discovery.

Company Description

Pioneering the discovery of membrane-permeable and orally-available cyclic-peptides with antibody-like binding affinity.

Bio

I am the co-founder and CEO of Insamo. Prior to founding Insamo, I completed a postdoctoral fellowship and earned an MBA while working with David Baker at the University of Washington. I earned my PhD at NYU, where I worked with Rich Bonneau (now Head of AI Molecular Design at Genentech) and Kent Kirshenbaum. Before graduate school, I held research positions at NASA, NIST, the FDA, and Merck.

Peptide Showcase
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Rashmin Savani
Co-Founder and Head, Scientific Advisory Board, Azome Therapeutics

RHAMM-derived Peptide Blocks NLRP3 Inflammasome Activation: Novel Therapy to Prevent Bronchopulmonary Dysplasia

Company Description

Background & Aims: The NLRP3 inflammasome is key in the pathogenesis of Bronchopulmonary Dysplasia (BPD), a devastating chronic lung disease in preterm infants. Hyaluronan (HA, hyaluronic acid), an endogenous danger signal, activates the inflammasome to produce IL1ß and promote inflammation. We have developed a peptide, AZM-152, derived from the HA receptor RHAMM that blocks NLRP3 inflammasome activation. We hypothesized that AZM-152 would block TLR-mediated cytokine elaboration in vitro and NLRP3 inflammasome activation in the neonatal mouse hyperoxia model of BPD.

Methods: The effect of AZM-152 on TLR-mediated activation of NFkB and IL1ß production was studied in cultured mouse and human macrophages using TLR4, TLR7, and TLR8 agonists. Neonatal wild type (WT) and RHAMM knockout (KO) mice were exposed to 95% oxygen from postnatal day (PN) 1 to PN5. WT mice were given increasing doses of AZM-152 subcutaneously on PN1. Myeloperoxidase activity (MPO, neutrophils) and N-Acetyl Glucosaminidase activity (NAG, macrophages), lung IL1ß mRNA and protein were determined. Alveolarization was determined using radial alveolar counts.

Results: RHAMM-based peptide AZM-152 inhibited all TLR-stimulated IL1ß expression. Exposure of neonatal mice to hyperoxia increased MPO and NAG activities, and IL1ß mRNA and protein. RHAMM KO mice failed to increase IL1ß and had no lung inflammation. Treatment of WT mice exposed to hyperoxia with AZM-152 resulted in dose-dependent inhibition of IL1ß and inflammation. AZM-152 treatment preserved alveolarization.

Conclusions: RHAMM is critical for NLRP3 inflammasome activation. AZM-152 prevents neonatal hyperoxia-induced increased IL1β and inflammation and preserves alveolarization. RHAMM antagonism is a potential therapeutic approach for the prevention of BPD and other inflammasome-driven diseases.

Bio

Rashmin C. Savani, MBChB, is the Chair of the Department of Pediatrics, holds the Nemours Eminent Scholar Chair at the University of Florida College of Medicine, and serves as Physician-in-Chief at the University of Florida Shands Children’s Hospital, Gainesville. Dr. Savani has an active laboratory investigating the basic mechanisms of lung development and injury in neonates with a focus on inflammation and angiogenesis as it relates to Bronchopulmonary Dysplasia, and on mechanisms of TLR activation of the NLRP3 inflammasome. He has published more than 100 peer-reviewed papers, reviews, and book chapters.

Sponsored Talk by Bachem
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Daniel Kessler
Sr. Group Leader Project Management, Bachem

CMC development for peptide API

Abstract

Developing peptide and oligonucleotide APIs demands a precise balance of efficiency, quality and compliance. To meet the growing demand for high-quality APIs for both clinical and commercial purposes, Bachem has established a comprehensive CMC development concept. This approach is tailored to each product, ensuring flexibility while maintaining rigorous standards. The concept involves a thorough analysis of process-related risks and ensures full alignment with both clinical timelines and regulatory guidelines.

Bio

Daniel is holding a Diploma in Biology and a PhD in Medicinal Biochemistry. He worked for 6 years as Postdoctoral Researcher in Molecular Cell Biology and Tumor Biology before he joined Bachem in 2013. As Senior Group Leader in Global Project Management, Daniel is heading a group of six Project Managers, focusing on CMC Development of Peptide APIs.

Peptide Showcase
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Wentao Guo
Technical Business Development - AI/ML solutions, Atombeat Inc.

Physics+AI-Guided Design and Plate-Based Synthesis Unlock >10¹² Cyclic Peptidomimetics for Cell-Permeable Inhibitor Discovery

Company Description

Cyclic peptidomimetics occupy the sweet spot between small molecules and biologics, combining high target affinity with proteolytic stability and intrinsic cell penetration. However, their vast chemical space presents significant challenges for discovery. To address this, we (Atombeat Inc.) introduce RiDYMO.PepTx, a physics- and AI-guided platform that enables rational in silica design within an in silico library of over 10¹² macrocycles, constructed from more than 500 natural and unatural amino acids. The platform integrates drug-likeness and permeability neural networks to prioritize candidates for rapid synthesis and testing.
We applied RiDYMO.PepTx to two contrasting targets: thrombin, where 8 of 89 compounds showed greater than 50% inhibition, and β-catenin, where 11 of 29 compounds demonstrated cellular IC₅₀ values below 10 µM. One β-catenin lead was confirmed to disrupt the BCL9 interaction, exhibit passive permeability, and inhibit Wnt signaling.
All hits emerged from a single design-make-test cycle, demonstrating how AI-enhanced, physics-informed design—coupled with parallel synthesis—can accelerate discovery and unlock challenging macrocyclic space.

Bio

Wentao Guo is a technical business development and product manager focused on AI/ML solutions at Atombeat Inc., a next-generation biotech company specializing in AI-driven and physics-based peptide and small molecule design. Wentao is a former postdoctoral researcher at Caltech and holds a Ph.D. in Computational Chemistry and an M.S. in Statistics.

Wentao aims to help translate AI capabilities into impactful scientific and life science applications. Serving as a bridge between technical teams, collaborators, and external partners, she plays a critical role in aligning project goals and model designs with effective execution. With an interdisciplinary background spanning pharmaceutical chemistry, physical chemistry, statistics, and deep learning, Wentao has contributed to the design and coordination of multiple AI models and deployment scenarios—particularly in scientific domains where cross-modality integration and precision modeling are essential.

Peptide Showcase
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Paul Wright
Senior Director, API Development and Manufacturing, Kailera Therapeutics

Kailera: Advancing Next-Generation Therapies for Obesity

Company Description

Kailera was launched in October 2024 with an experienced leadership team and a strong investor syndicate who possess a track record of building successful companies. Kailera is advancing a broad and advanced pipeline, including peptides and small molecules, which have the ability to help a broad range of obesity patients, including those with the highest unmet medical need (BMI 35+). This talk will provide an overview of the company and its assets.

Bio

Dr. Wright is a seasoned CMC leader with a PhD in analytical chemistry from the University of Cincinnati. He has served in several CMC cross-functional technical and management leadership roles at Eli Lilly and MBX Biosciences prior to joining Kailera as the Senior Director of API Development and Manufacturing.

Peptides in the Clinic
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Beverly Knight
Director, Johnson & Johnson Innovative Medicine

Translational Pharmacokinetics of Icotrokinra, an Orally Delivered Peptide that Inhibits the IL-23 Receptor

Abstract

IL-23 signaling inhibition via monoclonal antibodies has demonstrated efficacy and safety in patients with psoriatic disease and IBD.. Icotrokinra, a very potent targeted oral peptide that selectively inhibits IL-23 receptor signaling, was profiled in vitro and in vivo to elucidate its absorption, distribution, metabolism, and excretion (ADME) properties, as well as its drug-drug interaction potential.

Bio

Bev joined Janssen in 2018 as a Development DMPK leader. Early on, she had the opportunity to co-lead a Discovery team with the goal of identifying a stable peptide that could be orally delivered. The candidate was identified and rushed to the clinic in record time. This peptide has gone on to become a high-priority asset which just completed Phase 3. As a Therapeutic Area Lead (TAL) for Immunology within DMPK, she has oversight across the Immunology Discovery and Development portfolio and the DMPK project leads supporting these programs. She is also an active member of a cross-functional team which aims to identify and internalize novel oral modalities for drug delivery.

Prior to joining Janssen, she began her post-graduate career at Takeda, gaining drug discovery experience across several therapeutic areas over 6 years. This was followed by 5 years at Pfizer, working in Clinical Pharmacology, supporting both large and small molecule programs, including involvement in several biosimilar and ADC teams. She was also part of the team supporting a submission for Bosulif, and the submission, advisory committee meeting, and reapproval of the ADC Mylotarg.

Bev received a bachelor’s degree in chemistry, followed by a doctoral degree in Pharmacokinetics from the University of North Carolina at Chapel Hill. Her training and expertise focus on the intestine and drug absorption processes.

Spotlight on Discovery
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Christopher Ing
Chief Scientific Officer, ProteinQure Inc.

Structure-based Drug Design of a Novel Sortilin-Targeted Peptide Drug Conjugate with Efficacy in Preclinical Models of Breast Cancer

Abstract

Antibody drug conjugates (ADCs) have changed the clinical landscape for the treatment of advanced breast cancer. Despite their promise, ADCs face key limitations including
poor tumor penetration, a narrow therapeutic window, and challenges with linker and payload stability. Consequently, alternative targeted therapeutic modalities have emerged,
including peptide-conjugated drugs (PDCs) which can have dramatically different pharmacokinetic properties. The cell surface protein sortilin is a lysosomal trafficking
receptor that is overexpressed in a variety of cancers, including triple-negative breast cancer. We used computational methods to identify a targeting peptide for payload
delivery based on a fragment of the endogenous ligand progranulin. After verifying its binding, stability, and internalization properties, we discuss linker and conjugation
chemistry to support tumor-targeted delivery of a potent microtubule inhibitor, monomethyl auristatin E. We evaluate cytotoxicity of sortilin-targeting PDCs and their
efficacy in tumor growth inhibition in vivo. Structure-based design was employed to explore the importance of binding affinity and stability in a series of analogues. From
additional in vivo characterization, we identified a molecule (PQ203), with favorable potency, pharmacokinetics, and safety signals, which is undergoing IND-enabling studies
for a phase I clinical trial in 2025.

Bio

Chris is the co-founder and CSO of ProteinQure, a biotechnology company focused on the development of next-generation protein-based therapeutics. He received a PhD in Biochemistry at the University of Toronto focusing on structural biology and biophysics of ion channels, enzymes, and membrane receptors. Previously, he studied Theoretical Chemistry and Computational Physics at the University of Waterloo. He currently leads computational chemistry methods development and applications at ProteinQure, based in Toronto, Canada. He is passionate about cross-disciplinary collaboration to design novel synthetic protein libraries, new protein modalities, and better data-driven strategies for rational drug design.

Waleed Danho Young Investigator Award Ceremony & Keynote
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Anne Conibear
Assistant Professor, TU Wien

Posttranslational Modifications of Disordered Proteins

Abstract

The conformational flexibility of intrinsically disordered proteins and protein regions (IDRs), and their accessibility to modifying enzymes make IDRs hot-spots for protein regulation by posttranslational modifications (PTMs). Such PTMs increase the complexity of the proteome and can have central roles in regulating protein function, location, interactions and degradation. Little is known, however, about how PTMs modulate the conformations and interactions of IDRs, as they typically occupy multiple conformational states, have promiscuous interactions, and are often removed or poorly represented in structural biology studies. In this presentation, I will discuss our work towards understanding how PTMs modulate the conformations and interactions of IDRs. Protein synthesis and semi-synthesis provides access to site-specifically modified variants of IDRs, such as the HMGN1 and Tau proteins, and disordered termini of Hsp90 and β-catenin. These protein variants enable us to study the precise effects of PTMs and cross-talk of multiple PTMs on conformational populations using NMR spectroscopy. With these examples, I aim to show how integrating chemical protein synthesis with structural biology of IDRs allows us to gain new insights into the effects of PTMs on the conformation, dynamics and regulation of IDRs.

References:

[1] Conibear, A. C., Nat. Rev. Chem. 4, 674-695 (2020).
[2] Niederacher, G., Urwin, D.; Dijkwel, Y., Tremethick, D. J., Rosengren, K. J., Becker, C. F. W., Conibear, A. C., RSC Chem. Biol. 2, 537-550 (2021).
[3] Iebed, D., Gökler, T., van Ingen, H., Conibear, A. C., ChemBioChem, 25, e20241023 (2024).
[4] Gajsek, O., Becker, C. F. W., Conibear, A. C., Chem. Eur. J. e202403676 (2024).

Bio

Anne Conibear is an Assistant Professor at TU Wien (Technical University of Vienna, Austria). She is originally from Zimbabwe and completed her B.Sc.(Hons) and M.Sc. in Chemistry (2010) at Rhodes University, South Africa. She then moved to the University of Queensland, Australia with an International Postgraduate Research Scholarship for her PhD (2014) with Prof. David Craik. During her PhD, she started working with peptides and focused on the synthesis, structure and activities of cyclic disulfide-rich peptides from mammals, the theta-defensins. In 2014, she was awarded an Interdisciplinary Cancer Research (Marie-Curie co-fund) postdoctoral fellowship at the University of Vienna, Austria, and worked with Prof. Christian Becker on targeted immune-stimulating molecules for cancer therapy. She returned to the University of Queensland in 2019 with a UQ Development Fellowship to start her independent research on the synthesis and structure of posttranslationally modified proteins. In 2022, she took up a tenure-track Assistant Professor position in Peptide and Protein Chemistry at TU Wien, Austria. Research in her group focuses on how posttranslational modifications regulate protein structure and biological function of intrinsically disordered proteins and regions.

A.Santopretea, S.Mallartd, E. Bianchia R.Ingenitoa, P.Magottia, A.Brescianib, A.Di Marcoc, S.Espositoc, E.Monteagudoc, F.Carettic, L.Orsattic, D.Roversia, A.Santopretea, F.Tuccia, M.Venezianoc, D.Brasseurd, X.Chénédee, A.Corbiere, L.Gauzy Lazod, V.Gervatd, F.Marguetd, C.Minolettid, O.Pasquierf, B. Poiriere, A.Azame, P.Janiake, O.Duclosd, S.Illianoeg
IRBM, aPeptide Chemistry, bTranslational Biology cExperimental Pharmacology, Pomezia, Italy; Sanofi R&D, dIntegrated Drug Discovery, eCardio-Vascular and Metabolism, fDMPK, Investigative Toxicology Pre Clinical Safety Franceg Chilly Mazarin 91385 and Vitry sur Seine 94400, France

Targeting the relaxin family peptide receptor 1 (RXFP1) represents a promising strategy for the treatment of cardiovascular and renal diseases. We report the development of R2R01, a novel, long-acting peptide agonist engineered for high potency, extended half-life, and improved translational potential. Initial discovery efforts identified a C18 fatty acid–modified single-chain analogue of relaxin-2 (chain B) as a potent and selective RXFP1 agonist with favourable pharmacokinetic (PK)1-2 properties. However, advanced PK profiling of this compound highlighted elevated levels of oxidative metabolism occurring in dogs and minipigs, limiting further advancement3.
Through an extensive optimization program, we addressed these metabolic liabilities while maintaining sub-nanomolar RXFP1 activity. Structure-activity relationship (SAR) studies focused on modifying key molecular features—including fatty acid chain length, conjugation site, and linker composition. Notably, the introduction of α-methyl-lysine at position 30, along with additional stabilizing modifications, yielded analogs with enhanced metabolic stability, prolonged in vivo activity, and a significant reduction in mast cell–mediated pseudo-allergic reactions4.

R2R01 emerged as the lead candidate from this optimized series, exhibiting a best-in-class profile in terms of receptor potency, duration of action, and preclinical safety. Its development exemplifies the power of an integrated discovery platform combining rational design, high-throughput screening, and translational in vivo models to accelerate peptide therapeutic innovation. R2R01 is currently undergoing Phase 2 clinical evaluation in patients with heart failure and hepatorenal syndrome5, supporting its potential as a transformative therapy in areas of high unmet medical need.

1S.Mallart et al. J. Med. Chem. 2021, 64(4):2139-2150, 2S.Illiano et al. Sci. Rep. 2022, 12(1):20435, 3 S.Esposito. J. Pharm. Biomed. Anal. 2023, 227, 115256, 4S.Mallart et al. J. Med. Chem. 2025, 68, 3, 3873-3885, 5B.Poirier. Br. J. Pharmacol. 2024