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gangliosides (Nervomax / gangliosides, Fidia / Neurosido)

✓ Approved

Gramon · therapeutic agent

What is gangliosides?

gangliosides is a therapeutic agent developed by Gramon. It is approved for therapeutic indications via unknown.

Drug Profile

Brand NamesNervomax, gangliosides, Fidia, Neurosido
CompanyGramon
RouteUnknown
StatusApproved
Sources: ClinicalTrials.gov, Gramon

Therapeutic Indications

gangliosides is developed for 4 unique indications across 3 therapeutic areas.

Therapeutic AreaConditionPhase
Nervous system disordersDiabetic neuropathy✓ Approved
Nervous system disordersNeuropathy peripheral✓ Approved
Blood and lymphatic system disordersNeutropenia✓ Approved
Congenital, familial and genetic disordersRetinitis pigmentosa✓ Approved

Related Research Articles

PubMedInternational journal of biological macromolecules2026-08-28

Gangliosides GM3 and GD3 modulate insulin aggregation pathways and reduce cytotoxicity through structural remodeling.

Ahmad Nazifa Tasnim NT, Saha Jhinuk J, Mao Yimin Y, Silvers Robert R et al.

Insulin amyloid aggregation is a key pathological and pharmaceutical concern, particularly in the context of Type-2 Diabetes (T2D), where amyloid deposition can impair therapeutic efficacy and contribute to local tissue damage. While gangliosides are known to modulate amyloid formation in neurodegenerative systems, their influence on insulin aggregation remains largely unexplored. In this study, we investigate the effects of gangliosides GM3 and GD3 on insulin amyloid aggregation using Thioflavin-T (ThT) based fluorescence kinetics, Fourier Transform Infrared (FTIR) spectroscopy, Circular Dichroism (CD) spectroscopy, Small Angle X-ray Scattering (SAXS), Nuclear Magnetic Resonance (NMR) spectroscopy, and Transmission Electron Microscopy (TEM)to examine the aggregation pathway, changes in the secondary structure and morphology of insulin aggregates. Our results show that both GM3 and GD3 lipids accelerated insulin aggregation in a concentration-dependent manner while steering the pathway away from classical fibril formation, producing short, beaded structures distinct from the extended fibrils observed under lipid-free conditions. Structural analyses revealed distinct non-fibrillar intermediates with β-sheet-rich globular clusters in presence of GD3 and α-helical intermediates in GM3-treated samples. Notably, these ganglioside-induced aggregates exhibit significantly reduced cytotoxicity when compared to insulin-only aggregates. Furthermore, ganglioside-bound insulin species retain seeding capacity, suggesting that they can nucleate further aggregation despite their non-fibrillar morphology. These findings underscore the role of gangliosides in modulating insulin amyloid polymorphism and toxicity, offering new insights into their potential impact on the pathology of T2D and treatment strategies.

PMID 42665140
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PubMedNature communications2026-08-28

Cis glycan-glycan interactions organize membrane nanodomains that tune receptor signaling.

Suzuki Kenichi G N KGN, Komura Naoko N, Asano Sachi S, Takahashi Maina M et al.

The plasma membrane (PM) is generally viewed as organized by coordinated interactions among proteins and lipids, largely overlooking the cell's most extensive surface chemistry, the glycan layer. Here, we directly detect specific cis glycan-glycan interactions using single-molecule imaging of 39 chemically synthesized fluorescent ganglioside analogs in living cells and defined lipid bilayers. All gangliosides examined form transient, metastable homodimers via homophilic glycan interactions, which are stabilized by cholesterol to generate nanoscale ganglioside homodimer rafts. They represent fundamental organizing units underlying PM nano-heterogeneity. Using EGF receptor (EGFR) as a representative receptor, we show that the interactions of paired GM3 glycans in the GM3 homodimer raft with defined N-linked glycans on EGFR suppress ligand-independent EGFR dimerization by reducing the dimer formation rate and enhancing dissociation, and continue to slow dimerization after EGF stimulation. Our findings establish cis glycan-glycan interactions as an organizing principle of PM organization and receptor regulation.

PMID 42660957
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PubMedPharmaceutics2026-08-27

An Optimal Spray Device for the Nose-to-Brain Delivery of AmyP53, an Adaptive Therapeutic Peptide for Alzheimer's and Parkinson's Diseases.

Farias Gonçalo G, Chahinian Henri H, Hauchard Nathalie N, Brunet Dominique D et al.

Background: Nose-to-brain delivery offers a noninvasive route to bypass the blood-brain barrier for the treatment of neurodegenerative diseases. AmyP53 is a first-in-class adaptive 12-mer peptide that prevents the formation of neurotoxic amyloid oligomers by competitively targeting lipid raft gangliosides on brain cell membranes, thereby blocking the shared pathological mechanism underlying both Alzheimer's and Parkinson's diseases. Objective: Here, we report the identification of optimal spray devices for the nose-to-brain delivery of AmyP53, ahead of a planned Phase 1 clinical trial. Method/Results: Among six devices evaluated (four commercial systems and two novel devices specifically engineered for nose-to-brain delivery), two systems were identified as optimal for further clinical development (narrower plume angles and significantly higher deposition in the olfactory region): the Neurospray™ and Neurospray™ Preservative-Free (PF). AmyP53 was quantitatively and reproducibly delivered by both Neurospray™ systems, retaining full recognition of its therapeutic target (gangliosides), as assessed by a surface pressure-based ganglioside-binding assay. In a rabbit preclinical model, intranasal administration of AmyP53 with the Neurospray™ resulted in rapid and sustained brain delivery, detectable at 10 min and persisting at 24 h post-administration, without significant systemic exposure. Conclusions: These results validate the Neurospray™ drug delivery systems as optimal drug delivery systems for the clinical development of AmyP53.

PMID 42654104
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PubMedInternational journal of molecular sciences2026-08-27

MALDI Mass Spectrometry Imaging in Alzheimer's Disease Lipidomics: Matrix Selection, Spatial Lipid Pathology and Emerging Analytical Strategies.

Aebisher David D, Krzysztofińska Anna A, Smolak Barbara B, Bernat Patrycja P et al.

Alzheimer's disease (AD) involves not only amyloid-β and tau pathology but also extensive disturbances in lipid metabolism, membrane organization, neuroinflammatory signaling, and tissue homeostasis. Conventional lipidomics has identified changes in phospholipids, sphingolipids, sulfatides, ceramides, gangliosides, and cholesterol-related pathways, but tissue homogenization removes their anatomical context. The aim of this review is to critically assess how matrix selection, sample preparation, ionization polarity, and emerging analytical strategies influence the detection and interpretation of spatial lipid alterations specifically associated with AD neuropathology. Current evidence shows that AD-related lipid remodeling is region- and lesion-specific, with recurrent findings including ganglioside accumulation, sulfatide depletion, ceramide-related alterations, phospholipid remodeling, lysosomal lipid changes, and disturbed cholesterol homeostasis within or around amyloid plaques. Matrix chemistry strongly influences lipid-class coverage, ionization efficiency, spectral background, adduct formation, spatial resolution, and biological interpretation. Matrix-Assisted Laser Desorption/Ionization with Laser-Induced Post-Ionization (MALDI-2), ion mobility, reactive matrices, on-tissue derivatization, structural lipidomics, single-cell imaging, and spatial multiomics are expanding molecular coverage and annotation confidence. However, broader translation requires standardized workflows, structurally validated assignments, quantitative quality control, larger human cohorts, and improved interlaboratory reproducibility. Collectively, the available evidence indicates that the principal value of Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry Imaging (MALDI-MSI) in AD lies not merely in detecting altered lipid abundance, but in resolving lesion-specific lipid microenvironments whose interpretation depends directly on matrix chemistry, spatial resolution, and structural validation.

PMID 42653081
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PubMedThe Journal of membrane biology2026-08-25

From Meteorites to Membrane Rafts: Ganglioside-Incorporating Prebiotic Vesicles and the Emergence of Membrane Domain Organization.

Lefebvre Marine M, Chahinian Henri H, Lleshaj Aleksandra A, Roumaillac-Sargsyan Arthur A et al.

Life requires membranes. But what were the first membranes made of, and how did they acquire the functional complexity of modern cells? Here we show that nonanoic acid and nonanol, two short-chain amphiphiles found in carbonaceous meteorites, spontaneously incorporate gangliosides into their membranes, generating a ternary vesicle system that, under prebiotic-inspired conditions, recapitulates three hallmarks of eukaryotic membrane biology: (i) lateral membrane domain segregation consistent with lateral compositional heterogeneity analogous to liquid-ordered and liquid-disordered phase co-existence; (ii) ganglioside-dependent and charge-selective capture of cationic peptides, confirmed by both centrifugation-binding assays and Langmuir monolayer experiments; and (iii) inward membrane budding and intraluminal vesicle formation upon cationic peptide treatment, recapitulating multivesicular body biogenesis in a minimal molecular system. Molecular modeling reveals that the nonanoic acid/nonanol pair occupies a molecular volume equivalent to the sterane core of cholesterol, explaining its cholesterol-surrogate function. These findings demonstrate that lateral domain segregation, surface glycolipid asymmetry, and endocytic membrane remodeling are not evolutionary inventions; they are emergent physicochemical properties of amphiphile-glycolipid systems that predate cellular life itself.

PMID 42640294
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PubMedMethods in molecular biology (Clifton, N.J.)2026-08-19

Chemical Synthesis of Fluorescent Analogs of a- and b-Series Gangliosides.

Komura Naoko N, Ando Hiromune H

Fluorescent ganglioside analogs recently developed by our group using a fully chemical method have enabled the observation of the behavior, interaction, and lipid raft formation of gangliosides in cell plasma membranes at the single-molecule level. In this chapter, we describe the chemical synthesis of fluorescent analogs of a- and b-series gangliosides previously reported by our group. The procedures for key chemical reactions-glycosylation, global deprotection of gangliosides, and fluorescent labeling of gangliosides-are described in detail.

PMID 42613515
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