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Updated: Feb 13, 2026

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Gangliosides GM3 And GD3 Modulate Insulin Aggregation Pathways and Reduce Cytotoxicity Through Structural Remodeling.

Nazifa Tasnim Ahmad1,2, Jhinuk Saha1,2, Yimin Mao1

  • 1Department of Chemical and Biomedical Engineering, FAMU-FSU College of Engineering, 2525 Pottsdamer St., Tallahassee, FL 32310, United States.

Biorxiv : the Preprint Server for Biology
|February 12, 2026
PubMed
Summary
This summary is machine-generated.

Gangliosides GM3 and GD3 accelerate insulin aggregation, forming less toxic, non-fibrillar structures. These altered insulin aggregates retain seeding capacity, impacting Type-2 Diabetes (T2D) pathology and treatment.

Keywords:
CytotoxicityGangliosidesInsulin aggregationNon-fibrillar aggregatesPolymorphismType-2 Diabetes (T2D)

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Insulin amyloid aggregation is a critical concern in Type-2 Diabetes (T2D), affecting therapeutic efficacy and causing cell damage.
  • Gangliosides are known to influence amyloid formation in neurodegenerative diseases, but their role in insulin aggregation is understudied.

Purpose of the Study:

  • To investigate the impact of gangliosides GM3 and GD3 on insulin aggregation pathways and aggregate characteristics.
  • To determine the structural changes, cytotoxicity, and seeding potential of ganglioside-modified insulin aggregates.

Main Methods:

  • Utilized Thioflavin-T kinetics, FTIR, CD spectroscopy, SAXS, NMR, and TEM to characterize insulin aggregation.
  • Performed cytotoxicity assays to evaluate the toxicity of insulin aggregates in the presence and absence of gangliosides.

Main Results:

  • GM3 and GD3 accelerated insulin aggregation in a concentration-dependent manner, forming non-fibrillar, beaded structures.
  • Ganglioside-bound aggregates exhibited distinct secondary structures (β-sheet-rich globular clusters with GD3, α-helical with GM3) and significantly reduced cytotoxicity compared to insulin-only aggregates.
  • Despite altered morphology, ganglioside-bound insulin oligomers retained their seeding capacity.

Conclusions:

  • Gangliosides GM3 and GD3 modulate insulin amyloid polymorphism, reducing aggregate toxicity.
  • These findings offer novel insights into the role of gangliosides in T2D pathogenesis and potential therapeutic strategies.