Dr. Katerina Leftheris is currently a Biotech builder and executive leader. She holds a Visiting Professorship with Stony Brook University, is currently an SAB member and holds Board of Director positions for several biotech companies focused on peptides and macrocycles. She has spent over 25 years in the small molecule/macrocycle drug discovery and early development space from early screening for hits (HTS, DEL) Ph 1 clinical studies. Throughout her career, she and her teams have put 15 compounds into the Clinic spanning many molecular targets including (but not limited to) kinases, GPCR’s, NHR’s, protease inhibitors, E3 ligase modulators/ligand directed degraders, and integrins. These targets cover debilitating diseases in several therapeutic areas including oncology, I/O, immunology, neuroscience, metabolic diseases and fibrosis.
She was most recently the CSO of Vilya Inc, an Arch Ventures-backed biotech company advancing macrocycles as oral drugs using machine learning algorithms first developed by the D. Baker Lab (U. Washington). She built out a full in-house drug discovery team and advanced several targets using ML predictive docking algorithms. Prior, she held multiple positions including SVP for Drug Discovery, Rheos Medicines and VP of Discovery Chemistry at Pliant Therapeutics, While at Pliant, she built and led discovery teams and is co-inventor of multiple integrin inhibitors in the clinic including Bexotegrast, an orally active avb6/1 inhibitor currently in PhIIb/PhIII for Idiopathic pulmonary fibrosis and primary sclerosing cholangitis.
Earlier, Katerina was site-head of Discovery Chemistry for Celgene, San Diego, where she built and led chemistry teams in advancing five novel clinical candidates, including the then nascent degrader approach utilizing glutarimide CRBN binders. Prior, she held positions of increased leadership with Vitae Pharmaceuticals . Earlier in her career, Katerina held positions of increasing responsibility in Discovery Oncology and Immunology Chemistry at Bristol-Myers Squibb.
To date, Katerina has over 140 publications/issued patents. She is an elected ACS division councilor and sits on the Executive Committee of the MEDI division of the American Chemical Society.
Katerina earned her B.A. in chemistry from Smith College, Ph.D. in organic chemistry from the University of California, San Diego and completed an NIH Postdoctoral Fellowship, University of Pennsylvania.

There has been a significant resurgence in the advancement of peptides and macrocycles as therapeutic agents. This has been due in part to four main advances;
- Improved approaches for identifying hits (mRNA display, DEL, ML approaches)
- Discovery of novel approaches to drug delivery (permeation enhancers, sustained release formulations, etc.)
- The drug discovery of unique modalities requiring peptide/macrocycle binders such as drug conjugates and radioligand targeting agents.
- Renewed medicinal chemistry efforts targeting macrocycles/peptides
While these advances have yielded several clinical candidates, there are still significant unsolved challenges that continue to impede the overall drug discovery success rate. Often, the DMTA cycle is too long, in part due to lengthy, often challenging syntheses of peptides/macrocycle analogs off DNA. To improve cycle time, building blocks are often limited to what can be purchased, potentially limiting the diversity of structural motifs tested. The resulting hits frequently have poor ADME properties requiring an extensive medicinal chemistry effort. Also, routine delivery of bioactive peptides/macrocycles inside a cell remains a challenge. This talk will address some of these challenges and what novel approaches are currently in exploratory development. These include:
- The design of polymer-bound peptides that can penetrate a cell and show functional cellular activity as well as in vivo efficacy.
- A macrocycle-payload delivery system targeting the internalization of specific membrane bound proteins
- A machine learning engineered, nonribosomal screening approach that can generate peptides/macrocycles inside a cell

Marvin Albers holds a bachelor's degree in chemistry from Technische Universität Darmstadt (Germany) and a master's degree in chemistry from Universität Münster (Germany). During his master's studies, he participated multiple times in iGEM, the prestigious international synthetic biology competition that promotes interdisciplinary research and innovation. He also completed a one-year research stay at the Karolinska Institute in Sweden, where he gained advanced experience in molecular biology and translational research.

Since 2023, Marvin has been pursuing his PhD in the Grossmann Lab, where his research focuses on the structure-based design of RNA-targeting peptides. He also serves as the project leader of grabRNA, an initiative dedicated to developing next-generation RNA stabilizers to advance RNA delivery technologies.

Many diseases including various forms of cancer are not curable today since current therapeutics and modalities are not suitable to address the relevant biomolecular targets. Alongside the urgent need for new treatments in medicine, there is a growing demand for environmentally friendly innovations in agriculture, particularly for sustainable crop protection. In principle, RNA interference (RNAi) can enable the specific targeting of relevant biomolecules.This technology can be adopted and offers a highly specific and efficient tool to virtually suppress any desired target gene.

Despite RNAi’s vast potential, its broader application is hindered by significant challenges. Double-stranded RNA (dsRNA), the central component of RNAi, suffers from poor stability and limited cellular uptake. In relevant conditions, dsRNA is quickly degraded, reducing its effectiveness. Existing technologies have yet to provide a universal method to protect and stabilize dsRNA, limiting RNAi’s use in real-world applications.

Our innovative approach introduces a breakthrough solution based on synthetic peptides inspired by the tomato aspermy virus 2b (TAV2b) protein. These custom-designed peptides bind dsRNA, shielding it from degradation and preserving functionality. Once inside the cell, the peptides release the dsRNA in the reducing intracellular environment, allowing it to activate the RNAi machinery. Designed as a platform technology, our peptide stabilizers can bind any dsRNA sequence or length, making them broadly applicable across diverse fields. Their unique structure-specific interaction also allows seamless integration with existing RNA delivery systems, enhancing overall effectiveness.

RNAi is entering a new era and the field is advancing rapidly. However, delivery and stability remain the final barriers to widespread adoption. Our peptide-based stabilizers aim to overcome these hurdles. We are now demonstrating our technology in collaboration with global start-ups, unlocking RNAi’s full potential in medicine, biotechnology, and agriculture.

Shubhangini Singh Verma is a PhD student in IIT Guwahati, India. She has her expertise in both experimental and computational approaches. Her PhD work focuses on the development of peptide-based biocompatible hydrogels for biomedical applications. She is currently exploring short native peptides to design injectable hydrogels with promising potential in drug delivery and cell culture systems. Recently she has published a research article. In future, by integrating molecular design, characterization techniques, and in vitro evaluations, she aims to contribute to the development of next-generation biomaterials that are tunable, safe, and efficient.

A vast majority of peptide hydrogelators harbor a bulky, non-native aromatic moiety. Such foreign moieties raise safety concerns as far as biomedical applications of hydrogels are concerned. The hydrogel research, therefore, has branched to another dimension– to identify native or native-like short peptide stretches that could cause the gelation of biological fluids. Using well-defined criteria to identify native peptide stretches that could form a viscous solution in water but cause gelation of phosphate-buffered saline (PBS), we identified the hexapeptide stretch from human tau, viz. tau306–311, as a promising injectable hydrogelator. The peptide causes instant gelation of PBS and the cell culture media. Such hydrogels find applications as drug delivery vehicles, scaffolds for mammalian cell culture, wound-dressing material, etc.

Zhigao Niu holds a PhD (2016) in Pharmaceutical Science from the University of Santiago de Compostela, where his research focused on polymer and lipid-based nanoparticles for oral peptide delivery. Currently, Zhigao works at Novo Nordisk as Senior Scientist and Innovation Lead, responsible for external collaborations on new technologies covering oral biologics, long-acting injectables, high-dose/high-viscosity formulations, and tissue targeting, among others.
Zhigao's expertise and research interest involves advanced drug delivery systems and drug-device combinations for proteins, peptides and nucleic acids. He is an inventor of 3 patent families, and his work has been published in top pharmaceutical journals including the Journal of Controlled Release, Advanced Materials, ACS Nano, Advanced Drug Delivery Reviews. He is currently on the editorial board of Drug Delivery and Translational Research, and serves as peer reviewer for over 20 journals.

The current strategy for oral peptide delivery relies on the use of permeation enhancers (PEs). Despite the clinical success of a few peptide drug candidates, their overall bioavailability remains suboptimal. Our experience indicates that the local concentration of PEs is critical for enhancing the absorption of therapeutic peptides. However, most PEs are derived from fatty acids, which have limited solubility under physiological conditions. An example of this is SNAC, the enhancer utilized in the oral Semaglutide product.
To address the solubility issues associated with SNAC, we have explored various approaches while also aiming to promote a rapid onset of action to improve the current dosing conditions. We have assessed both liquid formulations, such as ionic liquids, and new solid tablet formulations in preclinical setups. The promising candidate has since been progressed to clinical evaluation. Additionally, factors that are likely to influence the performance of PE-based formulations as well as those contributing to clinical translatability issues will be shared.

John Phipps serves as the Vice President of Clinical Pipeline Development at CPC Scientific, boasting an extensive and distinguished track record in the pharmaceutical sector. His expertise spans biotechnology, chemistry, technology transfer, drug discovery, and protein chemistry, underpinned by a Bachelor of Science in Biochemistry from Colorado State University. John began his career in 1992 as a bench chemist and manager of the Colorado State University core facility from 1999 – 2001, making peptides by SPPS using Boc and Fmoc chemistry. In 2001, John founded Global Peptide Services, serving as president from 2001 to 2008. In 2010, he worked at Bachem as a business development manager until 2017. John joined to CPC Scientific in 2017, and he currently resides in Long Beach, California, and is available to engage peptide and oligonucleotide clients throughout the United States.

Semaglutide, a member of the GLP-1 class of anti-diabetic drugs, has received widespread attention in recent years due to its development as a treatment for obesity. While the current commercial supply utilizes recombinant DNA manufacturing technology, synthetic methods employing solid phase peptide synthesis (SPPS) and/or convergent peptide synthesis have been developed to produce a generic version of semaglutide. However, the non-enzymatic approach can result in poor product quality and low yields that stymie innovation and development.

To address this, CPC Scientific have designed and used the novel compound Fmoc-Gly-OtBu-FMPB that functions as a linker to AM resin and contains the C-terminal Gly31 required in semaglutide. This innovative approach suppresses formation of impurities, most notably those derived through formation of endo-Gly31-semaglutide. Through use of this novel linker and a convergent fragment-based approach, the purity of semaglutide peptide has been increased to 99.5% when preparing multiple-kilogram batches of the final API.

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.

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.

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.

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. Through a collaboration with Hengrui Pharmaceuticals, Kailera offers a broad and advanced pipeline, including peptides and small molecules, which have the ability to address 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 public information related to its assets.

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.

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.

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.

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

Danny Chou is an Associate Professor of Pediatrics (Endocrinology and Diabetes) at Stanford University. He received his PhD from Harvard University, working in the lab of Prof. Stuart Schreiber. His Ph.D. research involved the identification of suppressors of cytokine-induced apoptosis in pancreatic beta cells. He then moved to MIT, where he was a JDRF Postdoctoral Fellow in Department of Chemical Engineering. He worked under the guidance of Profs. Robert Langer and Daniel Anderson, focusing on the development of glucose-responsive insulin derivatives. Danny started his independent career in Department of Biochemistry at University of Utah in August, 2014. At Utah, Danny's research focused on protein and peptide therapeutics for the treatment in Type 1 Diabetes and other human diseases. In 2020, Danny moved his research lab to Stanford University to continue their efforts in developing novel insulin therapeutics. His laboratory has received funding support from NIH, DoD, JDRF and American Diabetes Association. Danny has received recognitions including an American Peptide Society Early Career Lectureship, Boulder Peptide Society Young Investigator Award, JDRF Career Development Award, Vertex Scholar, JDRF Postdoctoral Fellow and ADA Junior Faculty Award.

The area of insulin receptor (IR) antagonism represents a significant but largely untapped research field with a promising potential for advancing our understanding of insulin signaling, and consequently, driving the development of innovative therapeutic strategies for metabolic disorders. Despite the numerous studies on insulin analogs with agonistic properties—owing to their critical role in diabetes treatment—the investigations into IR antagonists are sparse. Our recent discovery of an antagonistic insulin derivative represents a promising starting point for developing new IR antagonists using structure-based designs. Using this strategy, we have been able to identify potent IR antagonists, which have been demonstrated to restore normoglycemia in disease models of hyperinsulinism.

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.

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).