Identification, structure-activity relationship and in silico molecular docking analyses of five novel angiotensin I-converting enzyme (ACE)-inhibitory peptides from stone fish (Actinopyga lecanora) hydrolysates

Autor: Chin Ping Tan, Shehu Muhammad Auwal, Najib Zainal Abidin, Nazamid Saari, Mohammad Zarei
Rok vydání: 2018
Předmět:
Reversed-Phase High Performance Liquid Chromatography
030309 nutrition & dietetics
Protein Conformation
Protein Hydrolysates
Peptide
Angiotensin-Converting Enzyme Inhibitors
Protein Sequencing
Physical Chemistry
Biochemistry
chemistry.chemical_compound
Computational Chemistry
Aromatic Amino Acids
Tandem Mass Spectrometry
Aromatic amino acids
Fractionation
Amino Acids
chemistry.chemical_classification
Liquid Chromatography
0303 health sciences
Multidisciplinary
Molecular Structure
Chemistry
Organic Compounds
Hydrolysis
Chromatographic Techniques
Fishes
Chemical Reactions
Molecular Docking
Molecular Docking Simulation
Separation Processes
Physical Sciences
Medicine
Hydrophobic and Hydrophilic Interactions
Research Article
In silico
Science
Molecular Dynamics Simulation
Research and Analysis Methods
Hydrolysate
03 medical and health sciences
Structure-Activity Relationship
Structure–activity relationship
Animals
Amino Acid Sequence
Molecular Biology Techniques
Sequencing Techniques
Molecular Biology
030304 developmental biology
Chemical Bonding
Organic Chemistry
Chemical Compounds
Biology and Life Sciences
Proteins
Hydrogen Bonding
Reversed Phase Chromatography
High Performance Liquid Chromatography
Isoelectric point
Docking (molecular)
Electrostatic Bonding
Peptides
Chromatography
Liquid
Zdroj: PLoS ONE
PLoS ONE, Vol 14, Iss 5, p e0197644 (2019)
ISSN: 1932-6203
Popis: Stone fish is an under-utilized sea cucumber with many health benefits. Hydrolysates with strong ACE-inhibitory effects were generated from stone fish protein under the optimum conditions of hydrolysis using bromelain and fractionated based on hydrophobicity and isoelectric properties of the constituent peptides. Five novel peptide sequences with molecular weight (mw) < 1000 daltons (Da) were identified using LC-MS/MS. The peptides including Ala-Leu-Gly-Pro-Gln-Phe-Tyr (794.44 Da), Lys-Val-Pro-Pro-Lys-Ala (638.88 Da), Leu-Ala-Pro-Pro-Thr-Met (628.85 Da), Glu-Val-Leu-Ile-Gln (600.77 Da) and Glu-His-Pro-Val-Leu (593.74 Da) were evaluated for ACE-inhibitory activity and showed IC50 values of 0.012 mM, 0.980 mM, 1.310 mM, 1.440 mM and 1.680 mM, respectively. The ACE-inhibitory effects of the peptides were further verified using molecular docking study. The docking results demonstrated that the peptides exhibit their effect mainly via hydrogen and electrostatic bond interactions with ACE. These findings provide evidence about stone fish as a valuable source of raw materials for the manufacture of antihypertensive peptides that can be incorporated to enhance therapeutic relevance and commercial significance of formulated functional foods.
Databáze: OpenAIRE
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