Posters

The enzyme Hyaluronidase catalyses the degradation of hyaluronic acid (hyaluronan), a major component of the extracellular matrix. In medicine hyaluronidase is used in combination with other drugs to lower the viscosity of hyaluronic acid, to increase the tissue permeability, to speed drugs dispersion and delivery. In cosmetic medicine it’s also used to dissolve hyaluronic acid dermal fillers. As market demand continues to rise there is an increasing need for manufacturing processes that are not only efficient but also robust and compatible with current Good Manufacturing Practice (GMP) standards. This need is especially critical when proteins are expressed in complex biological systems.

In this study, we present our developments in ligand discovery aimed at the targeted purification of Hyaluronidase. Using Navigo Pure’s proprietary Precision X® ligand libraries, we identified a set of affinity ligands tailored for the selective capture of this enzyme. The ligands were evaluated in the context of CHO supernatant and were characterized in terms of their binding affinity, target specificity and overall capture performance.

Our findings demonstrate that the selected ligands effectively enrich the target molecule while minimizing non-specific interactions, establishing a foundation for streamlined purification workflows. The underlying ligand platform Precision X® developed by Navigo Pure is designed to extend the advantages of Protein A affinity chromatography, traditionally applied to antibody purification, to the broader space of non-antibody biologics. Through our Precision Capturing® technology, we offer a novel and proprietary approach that enables simplified process architectures while maintaining high standards for yield and purity. This platform is particularly wellsuited for the purification of targets, where conventional methods often fall short in scalability, reproducibility, or regulatory compliance.

By enabling a more predictable and scalable purification strategy, Precision Capturing® provides a powerful tool for bioprocess development teams aiming to meet the rigorous demands of clinical and commercial manufacturing. It offers not only a high degree of operational robustness but also flexibility in adapting to diverse expression systems and process scales. This positions our platform as a unique solution for next-generation biologics manufacturing, supporting the advancement of novel peptide-based therapeutics from research through to GMP-compliant production.

© 2025 Published by Navigo Proteins GmbH

The ongoing clinical success of incretin-based peptide therapeutics, particularly glucose-dependent insulinotropic polypeptide (GIP) and glucagon-like peptide-1 (GLP-1) receptor agonists, has firmly established their therapeutic relevance in the treatment of type 2 diabetes and obesity. These peptides have demonstrated superior efficacy in improving glycemic control and promoting weight loss and remain the only class of drugs approved for both indications. Their dual effectiveness, coupled with favorable safety profiles, has intensified pharmaceutical and biotechnological interest in their large-scale production and commercialization. As market demand continues to rise, there is an increasing need for manufacturing processes that are not only efficient but also robust and compatible with current Good Manufacturing Practice (GMP) standards. This need is especially critical when peptide drug precursors are expressed in complex biological systems such as E. coli or yeast.

In this study, we present our initial developments in ligand discovery aimed at the targeted purification of two clinically validated incretin mimetics: Tirzepatide, a dual GIP/GLP-1 receptor agonist, and Semaglutide, a potent GLP-1 receptor agonist. Using Navigo Pure’s proprietary Protein A-derived ligand libraries, we identified a set of affinity ligands tailored for the selective capture of these therapeutic peptides. These ligands were evaluated in the context of clarified E. coli lysates, and were characterized in terms of their binding affinity, target specificity, and overall capture performance.

Our findings demonstrate that the selected ligands effectively enrich the target peptides while minimizing non-specific interactions, establishing a foundation for streamlined purification workflows. The underlying ligand platform developed by Navigo Pure is designed to extend the advantages of Protein A affinity chromatography, traditionally applied to antibody purification, to the broader space of non-antibody biologics. Through our Precision Capturing® technology, we offer a novel and proprietary approach that enables simplified process architectures while maintaining high standards for yield and purity. This platform is particularly well-suited for the purification of recombinant peptide therapeutics, where conventional methods often fall short in scalability, reproducibility, or regulatory compliance.

By enabling a more predictable and scalable purification strategy, Precision Capturing® provides a powerful tool for bioprocess development teams aiming to meet the rigorous demands of clinical and commercial manufacturing. It offers not only a high degree of operational robustness, but also flexibility in adapting to diverse expression systems and process scales. This positions our platform as a unique solution for next-generation biologics manufacturing, supporting the advancement of novel peptide-based therapeutics from research through to GMP-compliant production.

© 2025 Published by Navigo Proteins GmbH

Ferritin is a critical protein complex essential for iron storage and release in living organisms. Ensuring high purity and effective isolation of Ferritin is vital for its various biomedical and industrial applications. However, due to its low presence in human plasma, the purification of Ferritin can be very challenging.

The small amount of Ferritin (13-400 ng/mL) present in plasma makes purification a significant challenge for purification techniques. However, we have successfully overcome this challenge. Our next-gen Affinity Chromatography (AC) methods enable the isolation and purification of Ferritin with exceptional precision, ensuring high purity and yield even from very small initial amounts. This achievement underscores our commitment to leveraging cutting-edge technology to solve complex biochemical problems.

The development of AC for Ferritin purification is a significant bioprocessing advancement. This technique improves the efficiency of Ferritin isolation and ensures the production of high-quality Ferritin for applications in medical diagnostics and therapy. It can serve as a blueprint for many other antibodies, non-antibodies and proteins with clinical potential facing purification obstacles.

The custom affinity resin was developed using the Precision Capturing® technology. The platform brings the benefits of Protein A affinity chromatography to the space of non-antibody proteins. Precision Capturing® enables a simpler process architecture resulting in optimized purity and yield. It is a unique and innovative affinity technology for DSP development to achieve a robust, predictable, scalable, and GMP-compliant purification procedure.

© 2024 Published by Navigo Proteins GmbH and PreviPharma Consulting GmbH

The Receptor Binding Domain (RBD) of the spike protein of SARS-CoV-2 has shown promise for diagnosis, treatment, and development of vaccines for COVID-19. However, two problems persist with large scale production of RBD: 1) lack of high productivity upstream cell culture, 2) absence of a commercial, highly selective affinity resin. In an effort to overcome these limitations, we evaluated two novel technologies for the production and purification of RBD. Brieflccy, RBD was expressed using C1, an engineered fungal strain of Thermothelomyces heterothallica (Dyadic International1 ). The C1 platform expresses glycosylated antigens with high productivity, stability, and purity. RBD was purified using a novel affinity resin2 known to produce yields of 90% to 95% purity in one chromatography step. Affinity purification did not affect protein quality, as demonstrated by ACE-2 binding of RBD. The novel affinity resin showed excellent base stability, consistent product quality, and similar ACE-2 binding activity over 40 cycles. RBD produced in C1, in conjunction with affinity purification using a novel affinity resin, provides a breakthrough in the large-scale production of affordable COVID-19 protein-based vaccines.

© 2021 Dutta et. al.