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Biotecnol, PolyTherics Ally on Anticancer Tribody Drug Conjugates

Written by Peptide Therapy Guide Editorial TeamPublished September 9, 2026

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This guide cannot diagnose a condition or recommend a personal treatment plan. Discuss medical questions with a qualified professional.

Biotecnol and PolyTherics formed a collaboration that aims to develop multispecific anticancer Tribody-drug conjugates (TDCs) that consist of Biotecnol’s Tribody molecules linked to cytotoxic payloads attached using PolyTherics’ site-specific ThioBridge™ linker technology. The companies will evaluate the resulting ThioBridge Tribody-drug conjugates in preclinical cancer models, and jointly look for licensing partners for the most promising candidates.

PolyTherics’ ThioBridge platform has been developed to enable the conjugation of a range of therapeutic payloads to antibodies, antibody fragments, or scaffolds via specific sites and without impacting functional domains. “A key challenge facing developers of protein-drug conjugates is that the chemistry linking the targeting molecule to the toxic payload can lead to unstable, heterogeneous products,” remarks John Burt, PolyTherics’ CEO. “PolyTherics’ technology is site-specific, predictable, and results in stable and homogeneous conjugates. Combining these attributes with the versatility of Biotecnol’s Tribody platform has the potential to create the next-generation of targeted cancer therapies.”

Biotecnol’s Tribodies are multifunctional recombinant antibodies, generated via the natural in vivo heterodimerization of Fab fragments to form a scaffold, onto which two additional binding moieties can be incorporated, including scFv antibody fragments, natural protein ligands, cytokines, receptor domains, tags, or protein toxins, small molecules, or radionucleotides. The firm claims the resulting molecules are stable and easy to produce in a single batch, without the need for any post-production processing other than purification. Tribodies are in addition produced in standard mammalian cell technology using well established methods.

Biotecnol claims the technology has a number of advantages compared with other bispecific formats. In particular, trispecificity means one molecule can be dual-targeting with a T-cell effector function. And at about 100 KDa, the molecules are of a size that is between bispecific antibody fragments and IgG molecules, which the firm says represents an ideal balance between tumor penetration and half life. Its in-house pipeline includes Tribody candidates against triple-negative breast cancer, malignant melanoma, and gastric cancer.

PolyTherics is leveraging a suite of technologies for the site-specific conjugation of therapeutic proteins. It’s three-platform PEGylation technologies are TheraPEG™ for PEGylation across a native disulfide bond, CyPEG™ for PEGylation at a thiol on free cysteine, and HiPEG, for PEGylation at a histidine residue. The firm has also developed a low-viscosity polymer and glycopolymer for targeted delivery of therapeutic proteins.

Last month Pro Bono Bio exercised its option to take an exclusive global licence to PolyTherics’ TheraPEG technology for the development and commercialization of a TheraPEG-FVIII product. The option exercise follows a feasibility program to develop and evaluate a long-acting PEGylated form of Factor VIII for the treatment of hemophilia A.

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Related questions

01Undruggable or unscreenable?

Another obstacle to discovering new PPI inhibitors is the lack of libraries designed to hunt for them, points out Philippe Roche, PhD, senior scientist at the Integrative Structural and Chemical Biology team at the Cancer Research Center of Marseilles, France. “If you screen PPIs using libraries that were designed for kinases or GPCRs, that’s why you don’t get a lot of good results,” he says. To that end, his group began assembling a library focused on orthosteric inhibitors of PPIs. The result was 2P2Idb, a hand-curated, structural database cataloguing orthosteric inhibitors of PPIs for which the interface had been 3D characterized. From analyzing these known PPI inhibitors, and what structures they had in common, Roche and his colleagues developed a model to predict whether compounds would likely inhibit PPIs. Using this method, 2P2Idb creates an enriched screening library that dramatically increases the hit rate compared to standard libraries. Having proven their success with a small library of 1600 compounds, they are in the process of expanding the library to 10,000 compounds. Once that’s published, “the idea is to make this library available to labs around the world,” Roche says. “We will provide the library free of charge for people to be able to screen PPI targets.”

Source: www.genengnews.com ↗

02How stable is the antibody?

A crucial question often addressed during preclinical development focuses on the in vivo stability of therapeutic antibodies. Increasing the half-life of a therapeutic antibody has several benefits ranging from higher treatment efficacy to increased advantages for the patients who will have a fewer number of therapy sessions and a reduced cost. Given these compelling benefits, following the identification of therapeutic antibodies with the desired specificity, developers usually subject them to a refinement step to increase their stability. This process is often hindered by the lack of reliable experimental tools to predict the half-life of antibodies in patients. The major hurdle of using mouse models to predict antibody stability in the serum lies in the way immunoglobulin proteins are processed by the organism. In mammals, most proteins circulating in the serum undergo constant uptake by endothelial cells and are routed through the endosomes to the lysosomal compartment for degradation. In the endosomes, immunoglobulin G (IgG) proteins are recognized and bound by a transmembrane protein, called the neonatal Fc receptor (FcRn), which mediates their recycling to the plasma membrane and subsequent release back into the serum. As a result, the half-life of IgGs are significantly extended by this mechanism. Since most therapeutic antibodies belong to the IgG class, this recycling system is very relevant for their relative stability in the body. Remarkably, the relative affinity between IgGs and FcRn is extremely disparate between different species, with the mouse receptor showing a much higher affinity than its human counterpart.

Source: www.genengnews.com ↗

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Peptide Therapy Guide Editorial Team

Editorial team for Peptide Therapy Guide.

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