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BMS, Nordic Bioscience to Develop Biomarkers for NASH, Fibrotic Diseases

Bristol-Myers Squibb (BMS) and Nordic Bioscience said today they will partner to develop biomarker technology for diagnosis and monitoring of nonalcoholic steatohepatitis (NASH) and other fibrotic diseases. Under the collaboration—whose value was not disclosed

Written by Peptide Therapy Guide Editorial TeamPublished September 10, 2026

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Under the collaboration—whose value was not disclosed—the companies agreed to develop translational biomarkers and diagnostics for NASH in preclinical models of fibrotic diseases, as well as in clinical settings.

The partnership is designed to combine Nordic’s more than 25 years’ expertise in biomarker development and clinical trials, focusing extensively on fibrosis as well as rheumatology, with BMS’ drug-development efforts.

Fibrosis is one of the pharma giant’s five therapeutic areas of focus, along with oncology, immunoscience, cardiovascular, and “genetically defined” diseases caused by abnormalities in the genome.

BMS’ pipeline listed six pipeline candidates for fibrotic diseases as of January 1. Three of the six are in Phase II development: BMS-986020, a small-molecule lysophosphatidic acid 1 (LPA1) receptor antagonist; a recombinant human pentraxin-2 protein candidate for idiopathic pulmonary fibrosis and myelofibrosis that BMS acquired last year for up to $1.25 billion; and another biologic, PEG-FGF21 (pegylated human fibroblast growth factor 21), licensed by the pharma from Ambrx in 2011.

Another fibrosis-related indication for PEG-FGF21 is in Phase I, as are the other two other fibrotic disease candidates, both small-molecule compounds—a galectin-3 inhibitor and ND-L02-s0201, which targets heat shock protein 47 (HSP47).

ND-L02-s0201 is the lead candidate of Nitto Denko, which in November granted BMS an exclusive license to develop that candidate and other small interfering RNA (siRNA) molecules targeting heat shock protein 47 (HSP47).

“Addressing the significant need for better diagnostic and monitoring tools in fibrotic diseases is a key element of BMS’ fibrosis strategy to help patients suffering from these debilitating conditions,” said Mike Burgess, M.D., Ph.D., BMS’ head of cardiovascular, fibrosis, and immunoscience development, said in a statement.

Last week, BMS honed its therapeutic focus further by licensing its progressive supranuclear palsy (PSP) candidate BMS-986168 to Biogen, and its Duchenne muscular dystrophy candidate BMS-986089 to Roche. The deals could generate more than $1 billion for BMS.

Nordic Bioscience maintains a portfolio of more than 50 biomarkers, and has specialized in measurement, development, and validation of assays for collagens, elastins, and laminins as biomarkers of extracellular matrix (ECM) activity. The company invented C-terminal telopeptide (CTX), a biomarker that noninvasively identifies osteoporosis patients with a high rate of bone loss and can be used to assess response to osteoporosis therapy.

The company has also developed Protein Fingerprint™ technology, a method designed to identify and quantify disease-specific protein fragments that according to the company exceeds the specificity of gold-standard biomarkers in biological relevance and scientific rationale. The technology has been incorporated into assays that have identified disease-specific protein fragments, shown them to be different from normal intact proteins, and quantified them in body liquids, Nordic Bioscience said.

“There is a big unmet need in medical and drug development for simple noninvasive diagnostic, early proof-of-efficacy of intervention and prognostic biomarkers in the NASH field,” added Nordic Bioscience CEO Morten Karsdal, Ph.D.

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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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