ArticleMarine drugs2025
Preparation of Acetylcholinesterase Inhibitory Peptides from Yellowfin Tuna Pancreas Using Moderate Ultrasound-Assisted Enzymatic Hydrolysis.
Article in Marine drugs, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Effect of pulsed ultrasound pretreatment on enzymatic hydrolysis and bio-functional properties of luffa cylindrica seed protein hydrolysates.Ultrasonics sonochemistry · 2026Article
- Targeting the Cardiovascular-Alzheimer's Disease Axis: The Promise of Marine Bioactive Peptides.Marine drugs · 2026Review
- The Selectivity of Butyrylcholinesterase Inhibitors Revisited.Molecules (Basel, Switzerland) · 2025Review
- Studies on the Structure and Properties of Ultrasound-Assisted Enzymatic Digestion of Collagen Peptides Derived fromFoods (Basel, Switzerland) · 2025Article
- Bioactive Peptides Derived from Tuna: Screening, Extraction, Bioactivity, and Mechanism of Action.Marine drugs · 2025Review
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Bioactive peptides represent a promising therapeutic approach for Alzheimer's disease (AD) by maintaining cholinergic system homeostasis through the inhibition of acetylcholinesterase (AChE) activity. This study focused on extracting AChE inhibitory peptides from yellowfin tuna pancreas using moderate ultrasound-assisted enzymatic hydrolysis (MUE). Firstly, papain and MUE stood out from five enzymes and four enzymatic hydrolysis methods, respectively, by comparing the degree of hydrolysis and AChE inhibitory activity of different pancreatic protein hydrolysates. Subsequently, the optimal MUE conditions were obtained by single-factor, Plackett-Burman, and response surface methodologies. The pancreatic protein hydrolysate prepared under optimal MUE conditions was then purified by ultrafiltration followed by RP-HPLC, from which a novel AChE inhibitory peptide (LLDF) was identified by LC-MS/MS and virtual screening. LLDF effectively inhibited AChE activity by a competitive inhibition mechanism, with an IC
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Registered trials
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