Characterization of ACE Inhibitory Peptides from Mactra veneriformis Hydrolysate by Nano-Liquid Chromatography Electrospray Ionization Mass Spectrometry (Nano-LC-ESI-MS) and Molecular Docking
| Autor: | Yunhan Zhu, Rui Liu, Hao Wu, Lei Shi, Lingchong Wang, Xinzhi Wang, Jiao Chen |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
Spectrometry
Mass Electrospray Ionization ACE inhibitory peptide characterization nano-LC-MS/MS molecular docking Mactra veneriformis Protein Hydrolysates Electrospray ionization Pharmaceutical Science Angiotensin-Converting Enzyme Inhibitors Peptide Peptidyl-Dipeptidase A Molecular Docking Simulation Article Hydrolysate Drug Discovery medicine Animals Pharmacology Toxicology and Pharmaceutics (miscellaneous) lcsh:QH301-705.5 chemistry.chemical_classification Binding Sites Chromatography biology Active site Captopril Bivalvia Molecular Weight Biochemistry chemistry lcsh:Biology (General) Docking (molecular) biology.protein Peptides Chromatography Liquid Cysteine medicine.drug |
| Zdroj: | Marine Drugs; Volume 12; Issue 7; Pages: 3917-3928 Marine Drugs, Vol 12, Iss 7, Pp 3917-3928 (2014) Marine Drugs |
| ISSN: | 1660-3397 |
| DOI: | 10.3390/md12073917 |
| Popis: | Food-derived bioactive compounds are gaining increasing significance in life sciences. In the present study, we identified angiotensin I-converting enzyme (ACE)-inhibitory peptides from Mactra veneriformis hydrolysate using a nano-LC-MS/MS method. Mactra veneriformis hydrolysate was first separated into four fractions (F1–F4) based on molecular weight by ultrafiltration. The fraction with molecular weight lower than 1 kDa (F1) showed the highest ACE inhibitory activity. F1 was then analyzed by a high throughput nano-LC-MS/MS method and sequences of peptides in F1 were calculated accordingly. The 27 peptides identified as above were chemically synthesized and tested for ACE-inhibitory activity. The hexapeptide VVCVPW showed the highest potency with an IC50 value of 4.07 μM. We then investigated the interaction mechanism between the six most potent peptides and ACE by molecular docking. Our docking results suggested that the ACE inhibitory peptides bind to ACE via interactions with His383, His387, and Glu411 residues. Particularly, similar to the thiol group of captopril, the cysteine thiol group of the most potent peptide VVCVPW may play a key role in the binding of this peptide to the ACE active site. |
| Databáze: | OpenAIRE |
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