Publication: THE EFFECT OF LAMINARIN ON MICROGLIA DECTIN-1 IN THE PATHOGENESIS OF ALZHEIMER’S DISEASE: AN IN SILICO APPROACH
| dc.contributor.author | KAVIISH A/L VIJAYAKUMAR | |
| dc.date.accessioned | 2025-11-12T04:38:46Z | |
| dc.date.available | 2025-11-12T04:38:46Z | |
| dc.date.issued | 2025 | |
| dc.description.abstract | Alzheimer’s disease (AD) is a progressive neurodegenerative disorder characterised by amyloid beta (Aβ) plaque deposition and chronic neuroinflammation. Emerging evidence implicate microglial activation via pattern recognition receptors, particularly dectin-1, as a driver of immune dysregulation in AD. Laminarin, a marine-derived β-glucan, exhibits antioxidant and immunomodulatory properties, however, its potential to modulate neuroimmune receptor interactions remains underexplored. This study aimed to investigate whether laminarin can alter the interaction between dectin-1 and Aβ using an in silico approach. The three-dimensional (3D) structure of human dectin-1 was retrieved from public databases and sequentially docked with Aβ and laminarin using ClusPro and AutoDock Vina, respectively. The resulting ternary complex was subjected to 300-nanosecond molecular dynamics (MD) simulations using GROMACS. Structural stability and conformational changes were assessed through root-mean-square deviation (RMSD), root-mean-square fluctuation (RMSF) and radius of gyration (Rg), while binding free energies were estimated using the MM-PBSA method. Results showed that laminarin bound adjacent to the Aβ interface on dectin-1 with moderate affinity (–6.0 kcal/mol). Suggesting a potential allosteric rather than competitive interaction. MD simulations revealed that the laminarin-bound system had a lower average RMSD (3.03 nm) and a more compact conformation than the dectin-1- Aβ (unbound) system (3.37 nm). RMSF analysis revealed increased flexibility in loop regions associated with dectin-1 activation. MM-PBSA results further indicated enhanced van der Waals contributions and reduced electrostatic contributions, upon laminarin binding, indicative of an allosteric stabilisation mechanism. These findings suggest that laminarin may stabilise the dectin- 1-Aβ complex through conformational modulation, potential altering microglial signalling and attenuating neuroinflammation in AD. The study provides computational evidence supporting the immunomodulatory potential of laminarin and highlights its relevance as a candidate for further experimental validation in AD. Keywords: Alzheimer’s disease, laminarin, Dectin-1, amyloid beta, molecular dynamics, MM-PBSA, neuroinflammation, in silico | |
| dc.identifier.uri | https://hdl.handle.net/20.500.14377/37250 | |
| dc.language.iso | en | |
| dc.publisher | IMU University | |
| dc.subject | Alzheimer Disease | |
| dc.subject | Microglia | |
| dc.subject | Receptors, Pattern Recognition | |
| dc.subject | Molecular Docking Simulation | |
| dc.subject | Dectin-1 | |
| dc.subject | Amyloid beta-Peptides | |
| dc.subject | Molecular Dynamics Simulation | |
| dc.subject | Neuroinflammatory Diseases | |
| dc.title | THE EFFECT OF LAMINARIN ON MICROGLIA DECTIN-1 IN THE PATHOGENESIS OF ALZHEIMER’S DISEASE: AN IN SILICO APPROACH | |
| dc.type | Thesis | |
| dspace.entity.type | Publication | |
| oairecerif.author.affiliation | #PLACEHOLDER_PARENT_METADATA_VALUE# |