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Third Rock Ventures Sets Up New Firm Global Blood Therapeutics with $40.7M

Company’s SHAPE Platform will be used to discover small molecules that change the shape of key blood proteins. Third Rock Ventures has formed Global Blood Therapeutics with $40.7 million in Series A financing. The company’s SHAPE Platform has the ability to id

Written by Peptide Therapy Guide Editorial TeamPublished September 9, 2026

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Company’s SHAPE Platform will be used to discover small molecules that change the shape of key blood proteins.

Third Rock Ventures has formed Global Blood Therapeutics with $40.7 million in Series A financing. The company’s SHAPE Platform has the ability to identify oral, small molecule drugs that change the shapes of key blood proteins to modify their functions, enhance vital biological pathways, and drive therapeutic benefits.

The SHAPE Platform brings together advanced computational biology and protein-ligand modeling with medicinal chemistry and empiric screening capabilities focused on allosteric modulation. Global Blood Therapeutics is building a pipeline for severe, genetic blood diseases for which there are currently no effective cures and only extremely limited therapeutic options.

“Blood is one of the largest and most accessible organs and is a rich source of biologically and clinically validated targets,” remarks Mark A. Goldsmith, M.D., Ph.D., CEO of the new company and venture partner at Third Rock Ventures. “Global Blood Therapeutics aims to provide game-changing treatments for serious, genetic blood diseases that are well-understood but poorly served today by developing innovative medicines directed against clinically validated targets.

“Through our SHAPE Platform and our world-class team with a strong track record in science and drug discovery and development,” Dr. Goldsmith notes, “we are positioned to develop rapidly a new generation of safe and effective oral drugs that could truly change the treatment paradigm on behalf of patients.”

Founders of the company include Charles Homcy, M.D., and Craig Muir of Third Rock Ventures, David Phillips, Ph.D., co-founder of COR Therapeutics and Portola Pharmaceuticals, and three leading scientific researchers at the University of California, San Francisco: Matthew Jacobson, Ph.D., professor, pharmaceutical chemistry, Andrej Sali, Ph.D., professor, bioengineering and therapeutic sciences, and Jack Taunton, Ph.D., associate professor, cellular and molecular pharmacology.

Global Blood Therapeutics’ lead program focuses on sickle cell disease (SCD). It is caused by a point mutation in the hemoglobin beta chain, converting β6 glutamic acid to valine. When sickle hemoglobin (HbS) is deoxygenated, the replacement of β6 glutamic acid with valine results in a hydrophobic interaction with another hemoglobin molecule, triggering an aggregation into large polymers. The polymerization of deoxygenated HbS is the primary event in the molecular pathogenesis of SCD, resulting in a distortion of the red blood cell and a marked decrease in its ability to pass through the microvasculature. These rigid cells are responsible for the vaso-occlusive crisis that are the hallmark of the disease.

Global Blood Therapeutics is pursuing multiple drug discovery strategies for the treatment of SCD. In its lead program the company has identified small molecules that modulate the shape of HbS to a form that favors the oxygenated state. This approach may prevent the polymerization of HbS, allow the red blood cell to pass through the microvasculature, and improve the multiple pathologies associated with SCD.

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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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