From Sea to Lab: Angiotensin I-Converting Enzyme Inhibition by Marine Peptides—Mechanisms and Applications

Marine Drugs, Journal Year: 2024, Volume and Issue: 22(10), P. 449 - 449

Published: Sept. 30, 2024

To reveal potent ACE inhibitors, researchers screen various bioactive peptides from several sources, and more attention has been given to aquatic sources. This review summarizes the recent research achievements on marine with ACE-inhibitory action application. Marine are considered excellent bioactives due their large structural diversity unusual bioactivities. The mechanisms by which these inhibit include competitive binding ACEs’ active site, interfering conformational changes, avoiding identification of substrates. unique 3D attributes confer inhibition advantages toward activity. Because IC50 values peptides’ interaction low, structure-based assumes that between increased therapeutic Numerous studies focused sustainable extraction produced fish, mollusks, algae, sponges. Meanwhile, potential applications medical benefits worth investigating considering. Due exhibiting antioxidant, antihypertensive, even antimicrobial properties simultaneously, for cardiovascular disease other illnesses only increases. In addition, as show better pharmacological benefits, they have absorption rates low toxicity could perhaps be modified stability bioefficacy. Biotechnological advances in peptide synthesis formulation greatly facilitated generation peptide-based inhibitors subsequently offer new treatment models. article gives a complete assessment present state knowledge about organism inhibitors. it emphasizes relevance additional investigation into action, optimization manufacturing processes, vivo, preclinical, clinical settings, underlining urgency value this study. Using not broadens repertory compounds but also shows promise tackling global health burden caused diseases.

Language: Английский

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Antidiabetic Potential of Chinese Giant Salamander (Andrias davidianus)-Derived Peptide: Isolation and Characterization of DPP4 Inhibitory Peptides

Processes, Journal Year: 2025, Volume and Issue: 13(2), P. 453 - 453

Published: Feb. 7, 2025

Amid the global rise in type 2 diabetes, natural peptide-based therapies provide a safer alternative to synthetic drugs with fewer side effects. This study highlights antidiabetic potential of peptides derived from cultured Chinese giant salamander (CGS) meat hydrolyzed by Alcalase 2.4L FG through DPP4 inhibitory activity. The hydrolysate exhibited significant activity, an IC50 value 1317.0 ± 29.5 μg/mL. Using activity-guided modified-SPE fractionation, most potent peptide, PPAAQLL (PL7), was identified CGS alcalase hydrolysate, 230.1 4.9 μM. PL7 as non-competitive inhibitor enzyme kinetic studies, and intermolecular docking simulations suggested that it does not interact active site DPP4. Additionally, PL7’s stability against simulated gastrointestinal protease digestion its activity remains intact, indicating for effective oral administration. SRM quantification analysis revealed nearly six-fold enrichment RP-SPE fraction S1 compared crude underscoring effectiveness fractionation method. These findings highlight promising source managing diabetes. Future studies should focus on vivo efficacy, bioavailability, pharmacokinetics PL7.

Language: Английский

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Evaluation of novel angiotensin I-converting enzyme and dipeptidyl peptidase IV inhibitory peptides derived from yak milk based on peptidomics and network pharmacology

Food Bioscience, Journal Year: 2025, Volume and Issue: unknown, P. 106030 - 106030

Published: March 1, 2025

Language: Английский

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Exploring dipeptidyl peptidase‐IV inhibitory peptides from Tartary Buckwheat protein: A study of hydrolysis, fractionation, and molecular interactions

Journal of Food Science, Journal Year: 2024, Volume and Issue: unknown

Published: Dec. 1, 2024

Abstract Tartary buckwheat, a protein‐rich pseudocereal with anti‐diabetic effects, has not yet been fully explored as source of dipeptidyl peptidase‐IV (DPP‐IV) inhibitory peptides. This study aims to discover novel DPP‐IV peptides from tartary buckwheat protein (TBP). Five hydrolysis methods were employed, simulated gastrointestinal digestion (SGID) releasing the most active hydrolysates, showing both highest degree (22.66 ± 1.12%) and inhibition activity (41.81 1.52% at 1.25 mg/mL). In addition, ultrafiltration enriched <3 kDa fraction rate, further purification using reverse‐phase high‐performance liquid chromatography concentrated in first (F1). Nano chromatography‐tandem mass spectrometry analysis identified 10 new F1, among which peptide Leu‐His‐Ile‐Val‐Gly‐Pro‐Asp‐Lys (LHIVGPDK) exhibited strongest effect, an IC 50 value 1.61 mM. Kinetic studies revealed that LHIVGPDK acts mixed‐type inhibitor, molecular docking indicated it inhibits by forming stable complexes through five types interactions, hydrogen bonds playing key role. underscores TBP's potential properties, reinforcing beneficial food for diabetes management. Practical Application research effectively inhibit DPP‐IV, enzyme associated These findings suggest applications developing functional foods help control hypoglycemia.

Language: Английский

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