article · Journal of Receptors and Signal Transduction
Phycobiliproteins are dietary proteins that can serve as precursors to neuroprotective compounds aimed at multi-target management of Alzheimer's disease. Following simulated digestion in the gastrointestinal tract, three peptide fractions, designated P1, P2, and P3, were evaluated alongside phycocyanobilin through molecular docking simulations. The assessments examined interactions with key enzymes linked to neurodegeneration, including Beta-secretase 1, Glycogen synthase kinase 3 beta, Acetylcholinesterase, and Butyrylcholinesterase. Phycocyanobilin demonstrated strong binding affinities to Butyrylcholinesterase and Glycogen synthase kinase 3 beta, pointing to potential roles in addressing tau-related and late-stage cholinergic pathways. Meanwhile, peptide P2 showed notable affinity for Acetylcholinesterase and Beta-secretase 1, indicating potential influence over amyloidogenic and early cholinergic mechanisms. The peptides P1 and P3 offered complementary moderate activity across these targets, indicating that phycobiliproteins warrant deeper exploration as sources of bioactive compounds.
Alzheimer's disease involves several biological pathways, including protein accumulation and enzyme imbalances, making single-target treatments difficult. Identifying food-derived proteins that release diverse active peptides during digestion could help create preventive dietary strategies. This computational research highlights specific protein fragments that may simultaneously target multiple enzymes involved in cognitive decline.
This research could eventually inform the development of functional foods and nutraceutical products designed to support brain health. Potential users include food ingredient manufacturers and nutraceutical developers targeting cognitive health formulations. However, because the findings rely entirely on simulated digestion and computational molecular docking, the research represents an early discovery phase that requires experimental validation and clinical testing before commercial use is possible.
AI-generated from the published abstract. Always read the original work before citing.
Alzheimer's disease (AD) is a multifactorial neurodegenerative disorder characterized by amyloid-β (Aβ) accumulation, Tau hyperphosphorylation, and cholinergic dysfunction, necessitating multi-target therapeutic strategies. This study evaluated phycobiliproteins (PBPs) as dietary precursors of neuroprotective compounds acting on multiple AD pathways. After simulated gastrointestinal digestion, peptide fractions P1 (GCAPR), P2 (QAGDQL), and P3 (AGDASVL) were assessed alongside phycocyanobilin (PCB) using molecular docking against Beta-secretase 1, Glycogen synthase kinase 3 beta, Acetylcholinesterase, and Butyrylcholinesterase. PCB showed strong affinities toward BChE (-10.0 kcal/mol) and GSK-3β (-8.4 kcal/mol), suggesting modulation of tauopathic and late-stage cholinergic pathways. P2 exhibited notable binding to AChE (-8.8 kcal/mol) and BACE1 (-7.6 kcal/mol), indicating effects on amyloidogenic and early cholinergic mechanisms, while P1 and P3 provided complementary moderate activity. Overall, these findings support further investigation of PBPs as potential sources of bioactive compounds for functional food and nutraceutical applications targeting AD-related pathways.
This page summarises published work. The authoritative version sits with the publisher.
DOI: 10.1080/10799893.2026.2723004
Is something wrong with this record? Report it or request removal.
Discussion
Have you built on this work, tried to replicate it, or seen it applied in practice? Share what you know. Verified researchers and MARATTO™ domain experts can open a discussion, and any member can reply. Contributions are reviewed before they appear.
No discussion yet. Open the first thread.
New to MARATTO™? Create a free account.
