Exploration of the molecular interactions between angiotensin-I-converting enzyme (ACE) and the inhibitory peptides derived from hazelnut (Corylus heterophylla Fisch.)
| Autor: | Jing-Sheng Liu, Li Fang, Hongmei Li, Chunlei Liu, Weihong Min |
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| Rok vydání: | 2018 |
| Předmět: |
Tris
Size-exclusion chromatography Angiotensin-Converting Enzyme Inhibitors Peptidyl-Dipeptidase A Analytical Chemistry Cation–pi interaction chemistry.chemical_compound Corylus 0404 agricultural biotechnology In vivo medicine Animals Amino Acid Sequence Plant Proteins chemistry.chemical_classification Chromatography biology Hydrolysis Active site 04 agricultural and veterinary sciences General Medicine 040401 food science In vitro Molecular Weight Enzyme chemistry Mechanism of action Biochemistry biology.protein medicine.symptom Peptides Protein Binding Food Science |
| Zdroj: | Food Chemistry. 245:471-480 |
| ISSN: | 0308-8146 |
| DOI: | 10.1016/j.foodchem.2017.10.095 |
| Popis: | The mechanism of action of food-derived angiotensin-I-converting enzyme (ACE) inhibitory peptides has not been completely elucidated. In the present study, ion-exchange chromatography, gel filtration chromatography, reverse phase-high performance liquid chromatography, and liquid chromatography-electrospray ionization–tandem mass (LC-ESI-MS/MS) were employed for purifying and identifying the ACE inhibitory peptides from hazelnut. To understand the mode of action of these peptides, ACE inhibition kinetics, in vitro and in vivo bioavailability assays, active site analysis, and interaction between the inhibitory peptides and ACE were investigated. The results identified novel ACE inhibitory peptides Ala-Val-Lys-Val-Leu (AVKVL), Tyr-Leu-Val-Arg (YLVR), and Thr-Leu-Val-Gly-Arg (TLVGR) with IC50 values of 73.06, 15.42, and 249.3 μM, respectively. All peptides inhibited the ACE activity via a non-competitive mode. The binding free energies of AVKVL, YLVR, and TLVGR for ACE were −3.46, −6.48, and −7.37 kcal/mol, respectively. The strong inhibition of ACE by YLVR may be attributed to the formation of cation–pi interactions. |
| Databáze: | OpenAIRE |
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