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Gain Therapeutics Presents New Preclinical Data from its Gaucher Disease Program at the 19th Annual WORLDSymposium
Study results support the disease-modifying potential of GCase-targeting small molecule therapy for neuronopathic Gaucher disease BETHESDA, Md., Feb. 27, 2023
About this update from Gain Therapeutics, Inc.
[{"type":"text","content":"Study results support the disease-modifying potential of GCase-targeting small molecule therapy for neuronopathic Gaucher disease\nBETHESDA, Md., Feb. 27, 2023 (GLOBE NEWSWIRE) -- Gain Therapeutics, Inc. (Nasdaq: GANX) (“Gain”, or the “Company”), a biotechnology company transforming drug discovery with its proprietary computational discovery platform identifying novel allosteric binding sites and creating small molecule treatments, presented new pre-clinical data from its Gaucher disease program in a poster presentation at the 19th Annual WORLDSymposium held February 22–26, 2023, in Orlando, Florida. The data generated in an animal model of neuronopathic Gaucher disease (nGD) show that GT-02329 restores β-glucocerebrosidase (GCase) activity, depletes accumulation of toxic lipid substrates, reduces neuroinflammation and improves neuromuscular function. “These data are a further validation of the disease-modifying potential of our GCase-targeting small molecule compounds in diseases caused by mutations of the GBA1 gene, including for the treatment of nGD and GBA1 Parkinson’s disease,” said Matthias Alder, Chief Executive Officer of Gain. “The consistency of the extensive preclinical data package we have generated with our GCase-targeting drug candidates is encouraging, and we remain on track to submit the dossier for the start of the Phase 1 clinical study with our lead GCase-targeting compound GT-02287 in mid-2023.” The effect of Gain’s small molecule structurally targeted allosteric regulators of GCase that act on lysosomal function was shown in studies conducted in the conduritol beta epoxide (CBE) mouse model. CBE is a covalent inhibitor that causes a reduction in GCase activity by reacting with the catalytic site of GCase and inactivating the GCase enzyme, which results in neurological features that occur in nGD patients, including the accumulation of the toxic lipid substrate glucosylsphingosine. The data presented in the poster titled “GT-02329, a structurally targeted allosteric regulator of GCase, restores GCase activity, reduces microgliosis and improves fine locomotor skills in the CBE model of neuronopathic Gaucher’s disease” demonstrated that: GT-02329 is orally bioavailable and brain penetrant, restored GCase activity, reduced accumulation of GCase substrates glucosylceramide and glucosylsphingosine, reduced a marker...